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P. PROFMUREITHILEOPOLD. "Market Study Report on Bamba - Ganze -Vitengeni water Supply Project: Kilifi District Kenya Ministry of Water Development with S.M Ngola.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1982. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Global Environmental Accountability challenges for 21st century,A paper presented at annual Ward,kershaw and Minton environmental Law symposium held at the University of Maryland,USA April 28.".; 2000. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Effectively Increasing Employment an Agenda for Business. I.D.S Working Paper No. 152 Also privately circulated by S.G Hawkins and Associates.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Legal Framework for Conservation,ownership,Access and Utilization of African Biodiversity:Medical plant and Food Crops,A paper presented at the OAU scientific Technical and Research Commission/Kenya Industrial Property Office/Development partners workshop.". In: Law Journal,Issue No.4.; 1987. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. K, D. M, J. VL, G. G, J. M, S. M, L. H. "Factors associated with leg cleanliness of smallholder dairy herds in Kenya." East African Journal of Science, Technology and Innovation. 2019;1(1):11-26.
P. PROFMUREITHILEOPOLD. "Prospects and Challenges of NEPAD with Focus on Addressing Capacity Deficits. Working Document for the 7th Regional Consultative Meeting of UN Agencies working in Africa, Addis Ababa,.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2006. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""The Informal Economy and Micro and Small Enterprises in Africa: Instruments of Decent Work and Wealth Creation". Paper for the ILO/ARLAC Workshop on Poverty Reduction and Wealth Creation (Harare: April 2003).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "16. Professional Ethics: Fair Play and impartiality in Covering Elections .". In: Workshop on Effective Journalism in a Changing World: Fair and Impartial Coverage of Elections. United States International University Africa-Nairobi; 1996.
P. PROFMUREITHILEOPOLD. "Experience with Development planning in Kenya .". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Plant-level Industrial Relations in Kenya. A Case Study Papar written for ILO/SIDO African Labour Relations Project G.K. Ikiara and S.N Momanyi.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Employment, Technology and Industrialization in Kenya: A Study in Development Strategy. Dissertation Abstracts International Seriess A Vol. 35, No. 1.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "The Environmental Problems of Nairobi. A Paper presented at the first International Confrence on Urban and Sprartial Plannong of nairobi of Nairobi, held at Nairobi. Kenya on December 13-17, 19988 (Publiishes in 7(1/2) Africa Urban quartely 167.". In: Law Journal,Issue No.4.; 1992. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Regional Integration and Debt in East Africa. ISBN 0-07974-2803-8 (Harare: African Forum and Network on Debt and Development - AFRODAD, 2003).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "13. The Social Responsibility of the Electronic Media.". In: 10th Workshop on Broadcasting and Multi-Party Democracy . Nairobi, Kenya.; 1994.
P. PROFMUREITHILEOPOLD. "Labour Utilization and the Employment Problem in Africa in P. Ndegwa L>P. Mureithi and R.H Green Development Options for Africa in the 1980 and Beyond Nairobi Oxford University Press.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Report of Symposium on development Options for africa in the 1980 and Beyond with P. Ndegwa and R.H Green (Nairobi: Society for International Development and Afropress.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Economic Development Planning and Employment in English Speaking East and West Africa International Education Materials Exchange Geneva International Institute for Labour studies.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1978. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Environmental Impact Assesment:its Genesis, Evolution,Legal and Institutional Aspect and Relevance to Kenya,in Mwakio P. Tole (ed.) Environmental Impact Assessment in Kenya:Theory and Practice (Academy Science Publishers,Nairobi p.1.". In: Law Journal,Issue No.4.; 1997. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. KAAYAG. "The role of indigenous plant extracts in integrated control of African livestock ticks.". In: Proceedings of 9th International Veterinary Hemoparasite Disease Conference. Merida, Mexico; 1993.
P. PROFMUREITHILEOPOLD. "Experience with Development planning in Kenya Chapter 6 in M Urrutia and S. Yukawa Planning in Mixed Economies Tokyo: United Nations University and Oxford Press forthcoming.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1965. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Employment, Poverty Reduction and Wealth Creation Nexus in Africa.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "10. Media Approach: Journalistic Practices in Distributing Information on Health Care.". In: Training Course of East African Journalists on Primary Health Care Phase III. Dar-es-Salaam, Tanzania; 1987.
P. PROFMUREITHILEOPOLD. "Crisis and Recovery in African Agriculture: Prioritiew for Dialogue and Action Development seeds of change Vol.2/3.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1987. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Industrial Relations, Employment Promotion and Development Labour and Society Vol No I with a Gladstone & T. Mulat.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1979. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Measures for Regulation of Access to Genetic Resources and Benefit Sharing in Kenya ,A keynotr paper presented at the WWF/Government of Kenya National workshop on Access to Genetic Resources and Benefit Sharing in Kenya held at Nairobi,February 19-20.".; 1998. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. MRMAIMBAPATRICK. "F.K. Kong, S.Teng,, K.H. Tan, P.P. Maimba and L.W. Guan. Single-span, Continuous and Slender Deep Beams Made of High Strength Concrete.". In: Proceedings of the American Concrete Institute International Conference on High-performance Concrete, SP-149. Singapore, November 1994, pp.413-423. American Concrete Institute; 1994. Abstract

The principal objective of this study was to identify the factors that the management of verticaly integrated firms consider in making decisions to integrate either backword or forward. In order to meet this objective, the information sought for the study was collected through the use of a questionnaire. The sample consisted of 52 vertically integrated firms. 31 questionnaires were completed and provided the information used in this report. The study found out that he fator that influence a firm's decision to integrate vertically include certainity of demand for the firm's products, availability of adequate manufacturing facilities, investment costs, and the need for high market share. For textile and steel manufacturers, certain factor were important. The factors were: the need for improved co-ordination for a firm's activities, need for synergies, need for greater control over the firm's economic resources, level of competition in the industries and the mining firms, the need to control the firm's economic resources, the need to build new infrastructures, sze of buiness, and the level of competition in the industry are important

P. KAAYAG. "INSECT IMMUNE MECHANISMS: Their roles in vectorial capacity and efficacy of biological control agents.". In: Proceedings of Tanzania Entomological Association conference. Arusha, Tanzania; 1996.
P. PROFMUREITHILEOPOLD. "A Framework for Analysing Labour Absorption Capability of Different Firm Sizes in Kenya Manufacturing Working Paper No. 7.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1972. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Social Dialogue in Public Emergency Services: A Case Study of Kenya. WP.216, Print Version:92-2-115737-7 (Geneva: ILO Sector Programme, 2004).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2004. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "9. A Review of Health Communication Exercised by Mass Media in Kenya.". In: the Training Course of East African Journalists on Primary Health Care. Dar-es-Salaam, Tanzania; 1987.
P. PROFMUREITHILEOPOLD. "Some Issues in Economic Policy Reforms in Kenya". Paper prepared for the CRED Seminar on Economic Reforms and Liberalization in Africa at the Hilton Hotel, Nairobi.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1988. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "The Relationship between Population Employment and Economi Growth with an Illustration from Kenya. Population Employment and Economic Growth with an Illustration from Kenya. Prepared for the Rockefeller Founation Conference on population and Labour absorp.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1984. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Food Population and Rural Development in Kenya Progress Policies Problems and Prospects" Chapter 4 in Douglas Ensminger Food Enough or starvation for Millions Tata McGraw Hill,.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1980. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Urban Environmental Problem in Kenya in R Obutho (ed) environmeny and Development in kenya Urbanization and management of Kenya Urban Centres in the 21 Centry (Kenya National Academic if Sciences Nairobi.".; 1999. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. KAAYAG. "The potential of pathogenic fungi for tick control.". In: Proceedings of the parasitological society of southern African (PARSA) conference. University of Orange Free State, Bluefontein, R. S. Africa; 2000.
P. PROFMUREITHILEOPOLD. "Some Notes on sources of Machinery Inputs in Kenya papers written for the ILO/UNDP Employment Mission to Kenya.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1972. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Social Dialogue in Public Emergency Services.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2004. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Recommendations and Summary Proceedings of the 4th FKE/ILO Top Management PolicyWorkshop on Overcoming Obstacles to Employment in Kenya A Workshop Report. Prepared with J.C. Odaga & J. Barasa Nairobi Federation of Kenya Employers.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1988. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. 15. Professional Ethics: Fair Play Impartiality in Covering Elections. . Nairobi, Kenya.: United States International University (USIU) ; 1999.
P. PROFMUREITHILEOPOLD. "The Employment nexus in Kenya's Fifth Development plan 1984-88 in Frakklyn lisk (Ed.) Planning in Mixed Economies (Tokyo: United Nations University and Oxford Press forthcoming.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1984. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Investment Linkages of Rural Access roads in Kenya (Kenya Ministry of Transport and Communications November with B.P Finucane.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1982. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Africa and the Implementation of International environmental Law in University of Iowa College of Law Journal (Fall 2000,forthcoming)."; 2000. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Factor Intensity in Kenyas Industrial sector. An Input Ratio analysis. Working Paper No. 184. Instutute for Development Studies University of Nairobi.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Legislative Protectction of the Working Environment in kenya with Special Reference to Industry, an unpublished thesis submitted to the univesity of nairobi in partial fulfillment of the requirement fo the degree of Master of Law (Ll.m).". In: Law Journal,Issue No.4.; 1987. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Globalization Issues from a Developing Nations Perspective.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2005. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Tobacco-related Issues in Kenya" in WHO, Economic, Social and Health Issues in Tobacco Control (Kobe: World Health Organization, 2003).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. The Kenyan Primary Health Care Programmes and the Supportive Options for the Mass Media. Finland: , Geneva and University of Tampere,; Submitted.
P. PROFMUREITHILEOPOLD. "Employment Status and Gender in the Labour Market". Paper prepared for the NGO Forum for the UN Conference on the Women's Decade at Nairobi Kenya.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. K, A.N. K, W.E. M, E.G.M. M, D.N. K. "Diffuse Peritonitis Associated With Ventral Hernia In An Adult Doe: Case Report." IOSR Journal of Agriculture and Veterinary Science. 2014;7(1):53-55.
P. PROFMUREITHILEOPOLD. "Writings on the Economy of Kenya in Ole Norgaard Kenya in the Social Sciences An Annoteted Bibliography Nairobi Kenya Literature Bureau.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1982. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "New Directions in water legislation in Kenya/. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi.".; 2000. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Demographic and Technological Variables in Kenya's Employment Scene Eastern African Economic Review.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Globa Climate Change : The Third World Perspective, A paper read at the UN Association of Greater Boston Conference on the Greenhouse Effect- International and Domestic Reactions to Global Warming,held at the Boston College on April 27.". In: Law Journal,Issue No.4.; 1991. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. R, Schagen VB, Chakeredza S, Njoroge K, Kamau H, Baena M. "Teaching Biodiversity: A curriculum Guide for Higher Education.". In: Biodiversity International, Rome Italy.; 2011.
P. PROFMUREITHILEOPOLD. ""Preparing for the Future: Strategic Thinking and Long Term Planning". Paper presented at a DPMF Sensitization Workshop for Senior Policy Makers from EAC Countries (Addis Ababa: June 2003).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "14. Media and Democracy and Sustainable Development: .". In: The 10th Biennial Conference of the African Council for Communication Education . Accra, Ghana; 1994.
P. PROFMUREITHILEOPOLD. "Emploment and Options for africa in the 1980 and Beyond (Nairobi Oxford University Press. Edited with P. Ndegwa and R.H. Green.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "National Human Settlements Policies and Progremming in Kenya (Nairobi HABITAT.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Development Planning and Employment in Five West African Countries International Education Materials Exchange Geneva International Institute for Labour Studies,.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1977. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "The Effacacy of International Environmental Law-A personal Reflection.2 ILSA Journal of International and Comparative Law 61.". In: Law Journal,Issue No.4.; 1995. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "The Informal Economy and Micro and Small Business Enterprise in Africa.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "11. Training of Journalists and Democratic Transition in Kenya.". In: Journalism Seminar on Ethical Decision Making in News Processing in Multiparty Kenya. Nairobi, Kenya.; 1992.
P. PROFMUREITHILEOPOLD. "management for Development: Priority Themes in Africa Today (Nairobi: Oxford Unicweairy press1987 Co-editor and Contributor.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1987. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Scope and Some salient Features of Rural Employment in Kenya KIDMA: The Israel Journal of Development Vol.5, No.2.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1979. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Legal Framework for Conservation,ownership,Access and Utilization of African Biodiversity:Medical plant and Food Crops,A paper presented at the OAU scientific Technical and Research Commission/Kenya Industrial Property Office/Development partners workshop."; 1997. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. KAAYAG. "Biological control of livestock ticks using entomogenous fungi, Beauveria bassiana and Metarhizium anisopliae.". In: Proceedings of Tanzania Veterinary Association Scientific conference. Arusha; 1995.
P. PROFMUREITHILEOPOLD. "A survey of Pyrethrum Industry in kenya (1968) With S.K Gill M.Syanda and others.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1968. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Regional Integration and Debt in East Africa.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Kenya: Planning for the Quality of Life Work in Progress vol. 10, No. 2.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1987. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "9. The Media: Professional Independence and Fair Coverage of Elections Published in: Kenya Journal of Sciences: Series C. Humanities and Social Sciences ." Kenya Journal of Sciences: Series C. Humanities and Social Sciences . 1997;Volume 4 (No.1).
P. PROFMUREITHILEOPOLD. "The Effects of Higher Energy Costs on the Balance of Payments Employment Technology Choice and Real Incomes in Kenya with particular Emphasis on Machakos District a Report to the Ford Foundation with W. M Mwangi and H. Fieldstein.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Economic Efficiency and the Mechanisation of Small Farms in J.KG Mati Appropriate Mechanisation of Small Farms in africa (Nairobi Kenya National academy with B.A Ateng.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1980. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Garbage Imperialism:Transboundary Movement of Hazardous Wastes and International Law,5 Kenya National Academy Journal series C39.".; 1999. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. MRMAIMBAPATRICK. "Curriculum for NDT Course at University Level: A Kenyan Perspective.". In: Presentation paper for the International Atomic Energy Regional Training Workshop to Prepare Training Materials on Non-destructive Testing of Concrete Structures, Cairo, March 1998. The International Atomic Energy Agency; 1998. Abstract

The principal objective of this study was to identify the factors that the management of verticaly integrated firms consider in making decisions to integrate either backword or forward. In order to meet this objective, the information sought for the study was collected through the use of a questionnaire. The sample consisted of 52 vertically integrated firms. 31 questionnaires were completed and provided the information used in this report. The study found out that he fator that influence a firm's decision to integrate vertically include certainity of demand for the firm's products, availability of adequate manufacturing facilities, investment costs, and the need for high market share. For textile and steel manufacturers, certain factor were important. The factors were: the need for improved co-ordination for a firm's activities, need for synergies, need for greater control over the firm's economic resources, level of competition in the industries and the mining firms, the need to control the firm's economic resources, the need to build new infrastructures, sze of buiness, and the level of competition in the industry are important

P. KAAYAG. "Evaluation of a fungal formulation for control of ticks in vegetation.". In: Proc. Tanzania Vet.Association Annual Conference. Arusha; 1997.
P. PROFMUREITHILEOPOLD. "Measures affecting the Distribution Sector and Proposals to Improve its Performance. Paper written for the ILO/UNDP Employment Mission to Kenya.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1972. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Mainstreaming Labour and Employment Concerns Within the Framework of the New Partnership for Africa's Development (NEPAD): Issues, Initiatives and Actions." Keynote Address to a Forum of Permanent/Principal Secretaries, Directors-General and Commissioner.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2004. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Employment and Income Implications of Biotechnological Innovations in Kenya". Project paper written with B.F. Makau for ILO World Employment Programme.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1988. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "The Impact of Oil Price Increases on the Economy of Sub-Saharan African Countries Prepared with F.A Mahdi, C Sassanpour D.M Wai and S. Wangwe (Oxford: Centre for research on the New International Economic order.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1984. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Manpower and Employment in Kenya An Overview. Paper written with F.M Muhindi for the Ministry of Higher Education's Pre-investment Study on Business Education.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1982. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "(With G.M. Wamukoya) Environmental Management in Kenya:A Guide to the Environmental Management and Co-ordination Act 19999Centre for Research and Education on Environmental Law,Nairobi.".; 2000. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. KAAYAG. "Biocontrol of ticks using entomogenous fungi: Development of cheap fungal culture methods.". In: In proc. 3rd African Acarology Symposium. Cairo, Egypt ; 2004.
P. PROFMUREITHILEOPOLD. "A Production Function Analysis of Different Firm Sizes in Kenya. Working Paper No.183 I.D.S.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Globalization Issues from a Developing Nations Perspective". Paper for IFAC SMP/SME and Developing Nations Consultative Conference.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2005. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Labour Market Flexity and Employment in Africa.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2002. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Emploment promotion in the Informal Sector: Conceptual and Theoretical Issues". Paper prepresented at the ILO/JASPA Seminar on Employment promotion in the Informal Sector.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Employment, Technology and Industrialization in Kenya: A Study in Development Strategy. Dissertation Abstracts International Seriess A Vol. 35, No. 1.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1982. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "New directions in water Legislation in Kenya,A paper presentaed at the National Workshop on Environmental Governance in Kenya,held at the UNEP Headquaters,Gigiri,Nairobi,March 29-30.".; 2000. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Optimization with a Technological Constraint paper 4 in the Proceedings of the East african Universities Scial Science Conference (Kampala.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1974. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Environmental Law Administration and Working Conditions. A paper presented at the internation Labour Organization Federation of Kenya Employees Seminar on General and Working Environment, held at Nairobi Kenya on Septembae 25-29.". In: Law Journal,Issue No.4.; 1989. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. K, S.W. M, M.R. C, G. K, T.O. A, W.E. M, A.N. K, J.D. M. "A Retrospective Study on Findings of Canine Hip Dysplasia Screening in Kenya." Veterinary World . 2015;8(11):1326-1330 .
P. PROFMUREITHILEOPOLD. "Prospects and Challenges of NEPAD with Focus on Addressing Capacity Deficits.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2006. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Employment, Poverty Reduction and Wealth Creation Nexus in Africa". Paper for the ILO/ARLAC Workshop on Poverty Reduction and Wealth Creation (Harare: April 2003).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "The Importance of the Use of the Public and Private Media during the Election Process.". In: Eastern and Southern Africa Universities Research Programme (ESAURP). Arusha, Tanzania; 1996.
P. PROFMUREITHILEOPOLD. "Agriculture Development Council activities in Aasia Lessons for Kenya Report to the ADC the Ford Foundation and the University of Nairobi. Written with W.M Mwnagi S.E. Migot-Adholla and G.M Ruigu.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1985. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "The Industrialization Process and its Impact on Employment and Incomes in Kenya Paper written for ILO/JASPA with S.W Masai.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Estimating Capital Stock in Kenya. Paper presented at the 14th Conference of the International Association for Research in Income and Wealth in Aulanko, Finland.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1975. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "(With Joy Asiema)Indegenous peoples and Environment:The case of the Pastoral Masaai of Kenya, 5(1) Colorado Journal of International Environmental Law and policy 149.". In: Law Journal,Issue No.4.; 1994. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "Tobacco- Related Issues in Kenya.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "12. The Media and Multi-party Politics in Africa: The Case of Kenya.". In: The Media and Multi-party Politics forum .; 1990.
P. PROFMUREITHILEOPOLD. "Africa in the World Economy". Paper Presented at an OAU Workshop on Africa's Priorit Programme for Economic recovery (APPER) in Mombasa, Kenya.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1987. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Evaluation of the Institute of Cultural Affairs Contribution to Village Renewal Development Programme in Kenya with Particular Emphasis on Machakos district A Report to the Ford Foundation with W.M Mwnagi and II Fieldstein.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1983. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Editor of the Proceedings of an S.I.D Seminar on alternative Patterns of Development and Lifestyle in Eastern Africa with G.K Rukwaro.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1979. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "International Environmental Law:Emerging concepts and Principles,University of Nairobi.". In: Law Journal,Issue No.4.; 1997. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. PROFMUREITHILEOPOLD. "population Explosion: A Misnomer or Not Dialogue No. 1.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1965. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Preparing for the Future.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2003. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "10. Media Approach: Journalistic Practices in Distributing Information on Health Care.". In: Training Course of East African Journalists on Primary Health Care Phase III. Dar-es-Salaam, Tanzania; 1987.
P. PROFMUREITHILEOPOLD. "Some Thoughts on Management for Development Published in Management Journal of the Kenya Institute of Management.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1987. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "7. Press Freedom and The Functions of the Media in Kenya." the Journal of Africa Media Review . 1993;Volume 7 (No. 3 – December, 1993).
P. PROFMUREITHILEOPOLD. "Project Identification and Technolgy Choice with Perspectives from Kenya. Paper prepared for a working on Appropriate Technolgy held in Washington D.C.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1980. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "A Reviwe of the Current and prososed legal and institution frameworks for the Development and Protection of the Marine and Coastal Environment of Sub Sahara Africa A Keynote Paper prepared for conference on C0-Operative for the development and protection ."; 1998. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. MRMAIMBAPATRICK. "Structural Analysis, Structural Design and Concrete Technology .". In: International Atomic Energy Agency Regional Training Workshop on Preparation of Training Guidelines on Non-destructive Testing of Concrete Structures, Nairobi, May 1997. The International Atomic Energy Agency; 1997. Abstract

The principal objective of this study was to identify the factors that the management of verticaly integrated firms consider in making decisions to integrate either backword or forward. In order to meet this objective, the information sought for the study was collected through the use of a questionnaire. The sample consisted of 52 vertically integrated firms. 31 questionnaires were completed and provided the information used in this report. The study found out that he fator that influence a firm's decision to integrate vertically include certainity of demand for the firm's products, availability of adequate manufacturing facilities, investment costs, and the need for high market share. For textile and steel manufacturers, certain factor were important. The factors were: the need for improved co-ordination for a firm's activities, need for synergies, need for greater control over the firm's economic resources, level of competition in the industries and the mining firms, the need to control the firm's economic resources, the need to build new infrastructures, sze of buiness, and the level of competition in the industry are important

P. PROFMUREITHILEOPOLD. "Development in Practice Some reflections on Kenyas Experience. Working paper Nom 52 Institue for Development Studies, University of Nairobi.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1972. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Eastern and Central African Integration: What it Entails." Paper for Nairobi Stock Exchange (NSE) Golden Jubilee and 8th African Stock Exchanges Association (ASEA) Conference (Nairobi November 2004).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2004. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. "8. The Role of the Media in the Prevention and Control of AIDS in Africa.". In: The AIDS Epidemiology and Control Seminar .; 1988.
P. PROFMUREITHILEOPOLD. ""Africa: An Economic Outlook": Paper presented at an SGS International Trade Seminar at Safari Park Hotel, Nairobi.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1988. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Economic Plannig in Kenya. An Exploratory Introduction. Paper read at a UN University 's Workshop on Conditions Effective National Planning at Penang, Malaysia.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1984. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. "Patterns of Industrialisation in the Countries of the Indian Ocean Region in Alex kerr The Indian Ocean Region Resources and Development (perth University of Western Australia Press and Boulder Colorado Westview Press.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1981. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFSITUMAFRANCISD. "Criminal law (kenya Supplemental Management encylopaedia of laws Criminal Law (kuwer law international. The Hague.".; 1999. Abstract

New Directions in water legislation in Kenya?. A Paper presented as the National Workshop on environmental Governance in kenya, held at the UNEP Headquarters Gigiri, Nairobi, March 29-30. 2000

P. KAAYAG. "Novel methods in the control of ticks.". In: Proc. PARSA Conf, Golden Gate Highlands National Park, RS.Africa.; 2002.
P. PROFMUREITHILEOPOLD. "Non-farm Economic Activities rural Areas in Frank Child and Mary Kempe Small-Scale Enterprise I.D.S Occassional Paper No. 6.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1973. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. M. "informal financing mechanisms in urban areas in Kenya.". In: World Bank’s Urban Research Symposium. Washington D.C.; 2004.
P. PROFMUREITHILEOPOLD. "Eastern and Central African Integration.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2004. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. PROFMUREITHILEOPOLD. ""Labour Market Flexibility and Employment in Africa: Mixed Outcomes". Paper written for WB-FES-ILO/ACTRAV Capacity Building Seminar on Poverty Reduction Strategy Papers - PRSP (Lusaka).". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 2002. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. OCHILO. 16. The Growing Gap between Training and Employment in Communications in Anglophone Africa: Diagnostic and Strategies for Intervention in Tanzania, Kenya and Uganda. . Nairobi, Kenya.: UNESCO and ORBICOM INTERNATIONAL Network of UNESCO Chairs and Associates in Communications ; 1999.
P. PROFMUREITHILEOPOLD. "Growth linkages between Agriculture and industry in Kenya Journal of Eastern african Research and Development with K.L Sharma.". In: Gabbay R. &Siddique A., ed., Good Governance Issues and Sustainable Development: The Indian Ocean Region (New Delhi: Vedams Books). ISCTRC; 1984. Abstract
Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.
P. Ajuoga, A. Ogacho MAJMBO. Effects of concentration of dopant states on photactivity in niobium-doped TiO2. 24th July-4th August 2006, Dar es Salaam, Tanzania; 2006.
P. GICHANGI. "CD4 T-LYMPHOCYTES SUBSETS IN WOMEN WITH INVASIVE CERVICAL CANCER IN KENYA.". In: East African Medical Journal . Vol. Vol. 90 .; 2013:.
P. K. Gathumbi., V. S. Varma. GSJKDN. "Ocular neoplastic lesions of the horse in Kenya from specimens received between 1967 and 2013 in the University of Nairobi, Department of Veterinary Pathology Microbiology and Parasitology.". In: Kenya Veterinary Association 47th Annual Scientific Conference. Whitesands Hotel, Mombasa; 2013. Abstract

The objective of the study was to determine the trends in ocular tumours that affect the horse in
Kenya and to relate the histological characteristics to the clinico-epidemiological parameters.
The study design used the retrospective and prospective suspected cases presented to the
Department for histological diagnosis and from which a neoplastic diagnosis of the eye or its
adnexa was recorded. The procedure involved retrieval of diagnostic reports from retrospective
cases and histopathological examination of both retrospective and prospective cases. Each
case was evaluated for the type and frequency of histological lesions and clinicoepidemiological
data. Parameters included analyses of age, sex, breed, geographical origin,
diagnosis, location of neoplasms, the pathology of the lesion, and the clinical features
presented. The histological features were compared between cases and cellular behaviour was
correlated with clinico-epidemiological parameters.
The results showed that the most common ocular tumour was squamous cell carcinoma of the
adnexa. Occasional diagnosis included melanoma, adenoma, fibroma and lymphoma of the
adnexa. In a few cases, non neoplastic growths such as lymphoid hyperplasia of third eyelid
were key differential diagnoses. True ocular tumours were rarely observed.

P.D M, Gathungu GK, Njogu MK, Nyankanga RO, Ambuko J, Landeo JA. "Optimization of seed potato (Solanum tuberosum L.) tuber dormancy and sprouting capacity through integrated gibberellic acid and benzylaminopurine application." Journal of Agriculture and Ecology Research International . 2015;4(4):188-198.
P.E. O, W.M. A, D.W. N, K.O. O, H.O. R, J.R. W,.RC. L, Njagi S.M., Mumenya S.W. K’A. "Determination of Background Ionizing Radiations in Selected Buildings in Nairobi County, Kenya." Journal of Nuclear Medicine & Radiaion Therapy . 2016;7(3).
P.G J, and Yajnik A-AISKN. "Duodenal perforation following blunt abdominal trauma: A case report." East African Medical Journal . 1998;(75):669.
P.G. J. "Mucosal changes at the oesophago-gastric junction as visualized at Endoscopy–A prospective pilot study." MEDICOM-The African Journal of Hospital Medicine . Submitted;17(1):5-8.
P.K N. "Mitigating Engineering Profession Regulatory Gaps." Kenya Policy Briefs. 2021;2(2):73-74.
P.K BUNDI, JA O'o, J HASSANALI, P O. "Morphometry and variations of bony ponticles of the atlas vertebrae (C1) in a Kenyans.". In: Int. J. Morphol., 28(4): 1019-1024. Int. J. Morphol., 28(4): 1019-1024; 2010. Abstract

Atlas bridges, the bony outgrowths over the third segment of the vertebral artery are associated with compression of the artery and nerves. There are limited studies comparing morphometry of the complete atlas bridges and that of the ipsilateral transverse foramen. Bilateral and gender differences in the morphometry of the complete bridges remain relatively unexplored. One hundred and two atlas vertebrae (49 male and 53 female) obtained from the Osteology Department of the National Museums of Kenya were used for this study. The presence of complete posterior atlas bridge (retroarticular canal) and lateral bridge (supratransverse foramen)
was noted. Measurements were taken for the diameters of foramina, and the ipsilateral transverse foramina and their areas calculated. Complete posterior bridges occurred in 14.6% and 13.6% on the right and left sides respectively. The lateral bridge was found in 3.9% of the cases on the right side only. The complete posterior bridges had a cross-sectional area of 23.44mm2 on the right and 24.98mm2 on the left side. The lateral bridges had a mean cross-sectional area of 27.30mm2. The right and left transverse foramina had mean crosssectional
area of 36.30mm2 and 37.20mm2 respectively, which was significantly larger than that of the ipsilateral complete and posterior bridges. The smaller dimensions of the complete atlas bridges compared to the ipsilateral transverse foramen suggest that they may predispose to vertebrobasilar insufficiency, Barre-Lieou and cervicogenic syndromes due to compression of the contents in the foramina.

king'oo p.k. SMS based system to provide first aid information in Kenya. Nairobi: University of Nairobi; 2015.
P.K. T, Z. Q, G. N. "Estimation of blood loss after vaginal delivery." J. Obst. Gynae. East Central. Afr.. 2011;23(2):55-60. Abstract

Background: Thirty to thirty nine percent of maternal mortality is attributed to excess bleeding after childbirth. Amount of blood loss after childbirth is generally estimated visually though it is known that such estimates are grossly inaccurate. Locally, no studies had been done to assess the performance of visual estimation and direct measurement methods of estimating blood loss after delivery. This study aimed at estimating the amount of blood loss after childbirth using three different quantitative methods (visual estimation, direct measurement and laboratory determination). The study also aimed at establishing the incidence of Postpartum Hemorrhage (PPH) in a setting where Active Management of Third Stage of Labor (AMSTL) is practiced.

Objectives: To determine the amount of blood loss and the prevalence of PPH after vaginal delivery.

Design: Analytic cross-sectional study.

Setting: Pumwani Maternity Hospital (PMH) in Nairobi, Kenya.

Subjects and methods: One hundred thirty four pregnant women delivering vaginally at PMH were recruited and studied. Sampled pregnant women were interviewed using a structured data collection form, pre- and post delivery venous blood samples were taken for determination of hematocrit and blood loss after delivery estimated visually by the primary clinician conducting the delivery and directly measured by the researchers.

Main outcome measures: Visually estimated blood loss, directly measured blood loss and pre-and post-delivery hematocrit values.

Results: The mean age of the study population was 24.7 ± 4.8 years. The mean visually estimated, directly measured and laboratory determined blood loss was 121.1 ml, 300.2 ml and 257.0 ml respectively. Prevalence of PPH (blood loss ≥ 500 ml) by visual estimation was zero percent and 13.4% (95% Cl 5.3 - 21.5) and 11.2% (95% Cl 4.0 - 18.8) by direct measurement and laboratory determination respectively. Visual estimation consistently underreported the most significant risk factor for PPH was performance of an episiotomy.

Conclusion: Visual estimation is not sensitive and grossly underestimates the amount of blood loss after delivery, magnitude of underestimation increases with increasing amount of blood loss. Direct measurement of blood loss is both highly sensitive and specific in the detection of PPH.

P.L. P, G. M, M. W, J. O’ech, P. M. "The Cerebro-Placental ratio as a prognostic factor of foetal outcome in patients with third trimester hypertension." East and Central African Journal of Surgery . 2014;19(1):41-51.Website
P.M M, Okweba D. Combating new Piracy in the Indian Ocean. German: VDM Verlag Dr. Muller; 2012.
P.M M, Ndiritu J. Role of Parliament in Peacebuilding. VDM Verlag Dr. Muller, German ISNB 978-3-639-36651-8; 2011.
P.M M. "Peace and Conflict Studies in a global context ." Journal of Science Technology Education and Management (J-STEM) . 2011;3(No. 2):195-197.
P.M M, Muluka N. Communication Strategies in Disaster Management. VDM Verlag Dr. Muller, German ISBN 978-3-639358575; 2011.
P.M. MRWAMBUAPETER. "K. Onoe, K. Iwabuchi, C. Iwabuchi, H. Arase, S. Hatakeyama, P. P. Wambua, N. Fukushi, I.Negishi, R. A. Good and K. Ogasawara. Donor and Recipient specific tolerance in cells from Semi-Allogeneic, H-2 subregion compatible or Full Allogenic Bone Marrow Chim.". In: Immunobiology. 1989 Jun;179(2-3):172-89. IAHS Press Wallingford, UK.; 1989. Abstract

Specificities of tolerance induced in allogeneic bone marrow (BM) chimeras which had been established by injecting allogeneic BM cells pretreated with anti-Thy-1 mAb alone (without complement (C)) were analyzed using Simonsen's splenomegaly assay. Lymphocytes from fully allogeneic, semi-allogeneic and H-2 subregion compatible BM chimeras were specifically unresponsive to donor and recipient antigens (Ag). However, cells from H-2 subregion compatible chimeras initiated as vigorously a GVHR in F1 recipient mice, which were disparate at H-2K and I-A regions, as did spleen cells of donor mice, which were incompatible at the entire H-2 and minor histocompatibility regions of the recipients. The donor cells from such chimeras that initiated these considerable GVHR were either CD4+ or CD8+ T cells. Furthermore, synergistic effects by the CD4+ and CD8+ T lymphocytes were also observed. We found no evidence for a suppressive mechanism(s) in maintenance of the specific tolerance in allogeneic chimeras. Further, when lymphoid cells from these chimeras were adoptively transferred to irradiated mice of the donor strain and maintained for 5 days in the absence of recipient Ag (tolerogen), the adoptively transferred cells were shown to retain their unresponsiveness to the recipient Ag. These results reveal that T lymphocytes from allogeneic BM chimeras prepared by our method had been specifically induced to a tolerant state to both donor and recipient Ag and that the major mechanism of induction and maintenance of long-lasting tolerance is attributable to clonal deletion of both CD4+ and CD8+ T cell subsets rather than to the development of a population of suppressor cells of any sort.

P.M. MRWAMBUAPETER. "C. Iwabuchi, K. Iwabuchi, S. Kobayashi, K. Ogasawara, I. Negishi, B. Wang, P.P. Wambua, H.Arase, N. Fukushi, Y. Itoh, T. Gotohda, R. A. Good and K. Onoe. Deficiency in early development of the Thymus-Depended cells in irradiation Chimeras attributable to .". In: J Immunol. 1991 Jan 1;146(1):26-34. IAHS Press Wallingford, UK.; 1991. Abstract
Allogeneic bone marrow chimeras were prepared using reciprocal combinations of AKR and C3H mice. When C3H mice were recipients, the number of thymocytes recoverable from such chimeras (C3H recipient chimeras) was small as compared with that from chimeras for which AKR mice were used as recipients (AKR recipient chimeras) regardless of donor strain. The thymocytes from C3H recipient chimeras showed a profound deficiency in generating proliferative responses to stimulation by anti-CD3 mAb (2C11) or anti-TCR (alpha, beta) mAb (H57-597), even though the expression of CD3 and TCR molecules fell within the same range as that in AKR recipient chimeras. Furthermore, after stimulation with immobilized 2C11, the proportion of IL-2R+ cells in the thymocytes from C3H recipient chimeras was much less than that in AKR recipient chimeras. However, no significant difference in proliferative responses to 2C11 plus PMA, in influx of Ca2+ after stimulation with 2C11 or IL-2 production in response to 2C11 plus PMA or PMA plus A23187 was demonstrated between C3H and AKR recipient chimeras. These findings suggest that the thymocytes from C3H recipient chimeras have a deficiency in the signal transduction system as compared with chimeras for which AKR mice are the recipients. The thymic stromal component involved in this difference in the C3H recipient chimeras is discussed.
P.M. MRWAMBUAPETER, J PROFMULAAFRANCIS. "Aluvaala, E.K, Tsuma, L.M Wambua.P.P, Bulimo.W.D, and Mulaa F.J. Identification of Glycosyl Hydrolase producing Extremophilic bacterium using ribosomal DNA sequence. Sequence deposited at Gene Bank under accession number DQ 341411. (2006).". In: Gene Bank under accession number DQ 341411. IAHS Press Wallingford, UK.; 2006. Abstract
Although military conflicts are common on the African continent, there is a paucity of data regarding bomb-blast injuries in this region and in Kenya in particular. This paper describes the pattern of maxillofacial injuries sustained after the August 1998 bomb blast that occurred in Nairobi, Kenya. A retrospective cross-sectional study was carried out using hospital-based records of 290 bomb-blast survivors admitted at the Kenyatta National Referral and Teaching Hospital in Nairobi. Using a self-designed form to record information about variables such as the sex and age of the survivors and type of location of soft- and hard-tissue injuries, it was found that of the 290 bomb-blast survivors, 78% had sustained one or more maxillofacial injuries. Soft-tissue injuries (cuts, lacerations or bruises) were the most common, constituting 61.3% of all injuries in the maxillofacial region; 27.6% had severe eye injuries, while 1.4% had fractures in the cranio-facial region. This paper concludes that the effective management of bomb-blast injuries as well as those caused by other types of disaster requires a multidisciplinary approach. The high percentage of maxillofacial injuries confirm that maxillofacial surgeons should form an integral part of this multidisciplinary team.
P.M. MRWAMBUAPETER. "P. P. Wambua, F. D. Juma and W. Gitau. Sorbitol levels in normal Africans and in insulin depended diabetics. East Africa Med. J. Vol. No. 2, 99, 1988.". In: Immunobiology. 1989 Jun;179(2-3):172-89. IAHS Press Wallingford, UK.; 1988. Abstract

Specificities of tolerance induced in allogeneic bone marrow (BM) chimeras which had been established by injecting allogeneic BM cells pretreated with anti-Thy-1 mAb alone (without complement (C)) were analyzed using Simonsen's splenomegaly assay. Lymphocytes from fully allogeneic, semi-allogeneic and H-2 subregion compatible BM chimeras were specifically unresponsive to donor and recipient antigens (Ag). However, cells from H-2 subregion compatible chimeras initiated as vigorously a GVHR in F1 recipient mice, which were disparate at H-2K and I-A regions, as did spleen cells of donor mice, which were incompatible at the entire H-2 and minor histocompatibility regions of the recipients. The donor cells from such chimeras that initiated these considerable GVHR were either CD4+ or CD8+ T cells. Furthermore, synergistic effects by the CD4+ and CD8+ T lymphocytes were also observed. We found no evidence for a suppressive mechanism(s) in maintenance of the specific tolerance in allogeneic chimeras. Further, when lymphoid cells from these chimeras were adoptively transferred to irradiated mice of the donor strain and maintained for 5 days in the absence of recipient Ag (tolerogen), the adoptively transferred cells were shown to retain their unresponsiveness to the recipient Ag. These results reveal that T lymphocytes from allogeneic BM chimeras prepared by our method had been specifically induced to a tolerant state to both donor and recipient Ag and that the major mechanism of induction and maintenance of long-lasting tolerance is attributable to clonal deletion of both CD4+ and CD8+ T cell subsets rather than to the development of a population of suppressor cells of any sort.

P.M. MRWAMBUAPETER. "T. Gotohda, K. Ogasawara, P. P. Wambua and K. Onoe. Analysis of functional sites on a peptide antigen, in I.A. or I.E. - restricted T cell responses. International Immunology Vol. 3, No.6, 503, 1991.". In: J Immunol. 1991 Jan 1;146(1):26-34. IAHS Press Wallingford, UK.; 1991. Abstract
It has been shown that two different sites (an agretope and an epitope) on a peptide antigen function independently in T cell responses to the antigen. By virtue of these sites, antigens, MHC molecules, and TCRs constitute trimolecule complexes which eventually result in T cell activation. In our previous reports, we have defined that residues 46 and 54 on synthetic peptide composed of residues 43-58 of pigeon cytochrome c (p43-58, AEGFSYTDANKNKGIT) and its analogs function as an agretope and residue 50 as an epitope in both I-Ab and I-Ak-carrying mice. In the present study, to extend our method to the other MHC class II molecules (I-E), we used two peptide antigens, 46D50V54R and 50V54R, which had been prepared by substitution of amino acids at positions, 46, 50 and 54 or 50 and 54 of p43-58 D, V, R or V, R, respectively, and compared the immunogenicity with those of other peptide analogs. The 46D50V54R was shown to be non-immunogenic in I-Ab-carrying mice and the 50V54R was non-immunogenic in I-Ak-carrying mice. In contrast, the 46D50V54R or 50V54R could induce I-E-restricted proliferative responses of T lymphocytes in I-Eb/k- or I-Ek/k-carrying mice, respectively. Furthermore, residues 46 and 54 were shown to function as agretopes and residue 50 as an epitope in the I-E-restricted responses as they did in the I-A-restricted responses, even though some differences were seen between peptide-I-E interaction and peptide-I-A interaction. These agretopes and epitope functioned independently.
P.M. MRWAMBUAPETER. "P. P. Wambua, K. Iwabuchi, K. Ogasawara, Y. Itoh, H. Arase, M. Kajiwara, T. Gotohda, R. A.Good and K. Onoe. Comparative analysis of Thymnocyte and low density adherent cell functions. Microbiology and Immunology Vol. 38 ND 11 page 879 - 890, 1994.". In: Microbiology and Immunology Vol. 38 ND 11 page 879 - 890. IAHS Press Wallingford, UK.; 1994. Abstract
Thymocytes which have developed in the C3H thymus showed depressed proliferative responses to stimulation with anti-CD3 antibody as compared with those which have developed in the thymus of other strains of mice (i.e. AKR). The present study was conducted to analyze immunological functions of the thymic stromal cell population (low-density adherent cells, LDAC) in the C3H mice using allogeneic bone marrow (BM) chimeras established by BM transplantation in the reciprocal combination of AKR and C3H mice as donor or recipient. The thymic LDAC from C3H mice or the [AKR(donor)–>C3H(recipient)] chimeras contained a high proportion of Mac-1+ cells as compared to AKR mice or the [C3H–>AKR] chimeras. The proportion of Mac-1+ cells paralleled the IL-1- and PGE2-secreting ability of the LDAC cultured either in the presence or absence of LPS and also paralleled the antigen-presenting cell functions of the LDAC. Furthermore, after anti-CD3 stimulation the PGE2 inhibited more profoundly proliferative responses of [AKR–>C3H] or normal C3H thymocytes than those of the [C3H–>AKR] chimera or normal AKR thymocytes. A PGE2 inhibitor, indomethacin, reversed the depressed responses of the thymocytes which had developed in the C3H thymus. These findings suggest that the lower responsiveness of thymocytes from [AKR–>C3H] chimeras to anti-CD3 stimulation may be attributable to large amounts of PGE2 secreted by LDAC and/or to increased sensitivity of thymocytes themselves to PGE2.
P.M. MRWAMBUAPETER. "Abdi,A.I., Wambua P.P., Githui,E.K. and Bulimo, W.D. Nucleotide polymorphism in reqion I of the P.falciparum ebl-1 gene in field isolated obtained form various regions of Kenya (2007) in press.". In: International association of hydrological sciences ( IAHS) publication 2000 No 259. IAHS Press Wallingford, UK.; 2007. Abstract
Although military conflicts are common on the African continent, there is a paucity of data regarding bomb-blast injuries in this region and in Kenya in particular. This paper describes the pattern of maxillofacial injuries sustained after the August 1998 bomb blast that occurred in Nairobi, Kenya. A retrospective cross-sectional study was carried out using hospital-based records of 290 bomb-blast survivors admitted at the Kenyatta National Referral and Teaching Hospital in Nairobi. Using a self-designed form to record information about variables such as the sex and age of the survivors and type of location of soft- and hard-tissue injuries, it was found that of the 290 bomb-blast survivors, 78% had sustained one or more maxillofacial injuries. Soft-tissue injuries (cuts, lacerations or bruises) were the most common, constituting 61.3% of all injuries in the maxillofacial region; 27.6% had severe eye injuries, while 1.4% had fractures in the cranio-facial region. This paper concludes that the effective management of bomb-blast injuries as well as those caused by other types of disaster requires a multidisciplinary approach. The high percentage of maxillofacial injuries confirm that maxillofacial surgeons should form an integral part of this multidisciplinary team.
P.M. MRWAMBUAPETER. "P.H. Rees, P.A. Kager, M.R. Murithi, P.P. Wambua, S.D. Shah and A.E. Butterworth. Tuberculin sensitivity in Kala-azar. Transaction of the Royal Society of Tropical Medical and Hygiene: Vol. 75 No. 5,630, 1981.". In: Immunobiology. 1989 Jun;179(2-3):172-89. IAHS Press Wallingford, UK.; 1981. Abstract

Specificities of tolerance induced in allogeneic bone marrow (BM) chimeras which had been established by injecting allogeneic BM cells pretreated with anti-Thy-1 mAb alone (without complement (C)) were analyzed using Simonsen's splenomegaly assay. Lymphocytes from fully allogeneic, semi-allogeneic and H-2 subregion compatible BM chimeras were specifically unresponsive to donor and recipient antigens (Ag). However, cells from H-2 subregion compatible chimeras initiated as vigorously a GVHR in F1 recipient mice, which were disparate at H-2K and I-A regions, as did spleen cells of donor mice, which were incompatible at the entire H-2 and minor histocompatibility regions of the recipients. The donor cells from such chimeras that initiated these considerable GVHR were either CD4+ or CD8+ T cells. Furthermore, synergistic effects by the CD4+ and CD8+ T lymphocytes were also observed. We found no evidence for a suppressive mechanism(s) in maintenance of the specific tolerance in allogeneic chimeras. Further, when lymphoid cells from these chimeras were adoptively transferred to irradiated mice of the donor strain and maintained for 5 days in the absence of recipient Ag (tolerogen), the adoptively transferred cells were shown to retain their unresponsiveness to the recipient Ag. These results reveal that T lymphocytes from allogeneic BM chimeras prepared by our method had been specifically induced to a tolerant state to both donor and recipient Ag and that the major mechanism of induction and maintenance of long-lasting tolerance is attributable to clonal deletion of both CD4+ and CD8+ T cell subsets rather than to the development of a population of suppressor cells of any sort.

P.M. MRWAMBUAPETER. "K. Ogasawara, P.P. Wambua, T. Gotohda and K. Onoe. Modification of the T cell responsiveness to synthetic peptides by substituting amino acids on agretopes. International Immunology. Vol. 2, No.3, 219, 1990.". In: International Immunology. Vol. 2, No.3, 219, 1990. IAHS Press Wallingford, UK.; 1990. Abstract
T cell receptors, major histocompatibility complex molecules, and antigens constitute tri-molecular complexes which induce T cell activation. T cells in I-Ab mice generate proliferative responses to a synthetic peptide composed of residues 43-58 of pigeon cytochrome c (p43-58) and its analogs with substitution at position 50 (50A, 50V, 50L, 50N, 50Q, 50K, and 50M). However, none of these peptides stimulate T cells in I-Ak mice. We substituted two residues at positions 46 and 54 of p43-58(50D), 50V, 50L, 50E, and 50K with two amino acids on agretopes of the I-Ak binding HEL52-61 peptide and immunized I-Ak mice with these newly synthesized peptides: 46D50D54R, 46D50V54R, 46D50L54R, 46D50E54R, and 46D50K54R. Apart from 46D50D54R, these peptides elicited T cell responses in I-Ak mice in an immunogen-specific manner, but did not stimulate those in I-Ab mice. Further, 46D50V54R inhibited competitively the responses of I-Ak restricted T cell hybridomas specific for 46D50E54R. These results demonstrate that the residues at positions 46 and 54 on the peptides act as an agretope and the residue at position 50 acts as an epitope in I-Ak mice, as in I-Ab mice, and provide the possibility of opening up a new method to prepare peptide antigens which induce T cell responses in each murine strain by introducing appropriate amino acids on agretopes.
P.M. MRWAMBUAPETER. "P.P Wambua. Functional and Phenotypic analysis of thymic low density adherent cells from murine bone marrow chimeras - Influence on thymocyte differentiation. The Hokkaido Journal of Medical Sciences, Vol. 67, No. 3 1992.". In: The Hokkaido Journal of Medical Sciences, Vol. 67, No. 3. IAHS Press Wallingford, UK.; 1992. Abstract
Previous studies from this laboratory demonstrated a malfunction of the thymus of C3H mice to induce normal level of thymocyte differentiation. Thymocytes developed in the C3H thymus showed depressed proliferative responses to stimulation with anti-CD3 antibody compared with those developed in the other strains. This study was conducted to analyze immunological functions of the thymic stromal cell population in the C3H mice. Using allogeneic bone marrow (BM) chimeras established by reciprocal combination of AKR and C3H mice as donor or recipient, antigen presenting cell (APC) function of low density adherent cells (LDAC) in the thymus was analyzed. The thymic LDAC from C3H mice or [AKR––C3H] BM chimeras where AKR were BM donors and C3H were recipients contained high proportion of Mac-1+ cells as compared to AKR mice or [C3H––AKR] chimeras. The proportion of Mac-1+ cells paralleled the IL-1 secreting ability of the LDAC. Thus, the higher proportion of Mac-1+ cell in the thymus may be responsible for low accessory function observed in C3H thymuses. However, when APC function was analyzed using various T cell hybridomas or a T cell line, the APC functions did not necessarily correlate to the proportions of Mac-1+ cells and amounts of IL-1 produced by the LDAC. When proliferative responses of thymocytes to anti-CD3 stimulation were analyzed in the presence of prostaglandins, PGE-2 inhibited more profoundly the responses of [AKR––C3H] and normal C3H mice than those of [C3H––AKR] and normal AKR mice. Furthermore, a prostaglandin inhibitor, indomethacin, reversed the depressed responses of the former thymocytes which had developed in the C3H thymus. These findings suggest that the hyporesponsiveness of thymocytes from [AKR––C3H] chimeras to anti-CD3 stimulation may be attributable to their increased sensitivity to prostaglandin produced by LDAC.
P.M. MRWAMBUAPETER. "Abdi,A.I., Wambua P.P., Githui,E.K. and Bulimo, (2007). Deposited 35 P.falciparum ebl-1 gene variants at Gene Bank. Received provisional accession numbers for each gene: EF205091-EF205127.". In: International association of hydrological sciences ( IAHS) publication 2000 No 259. IAHS Press Wallingford, UK.; 2007. Abstract
Although military conflicts are common on the African continent, there is a paucity of data regarding bomb-blast injuries in this region and in Kenya in particular. This paper describes the pattern of maxillofacial injuries sustained after the August 1998 bomb blast that occurred in Nairobi, Kenya. A retrospective cross-sectional study was carried out using hospital-based records of 290 bomb-blast survivors admitted at the Kenyatta National Referral and Teaching Hospital in Nairobi. Using a self-designed form to record information about variables such as the sex and age of the survivors and type of location of soft- and hard-tissue injuries, it was found that of the 290 bomb-blast survivors, 78% had sustained one or more maxillofacial injuries. Soft-tissue injuries (cuts, lacerations or bruises) were the most common, constituting 61.3% of all injuries in the maxillofacial region; 27.6% had severe eye injuries, while 1.4% had fractures in the cranio-facial region. This paper concludes that the effective management of bomb-blast injuries as well as those caused by other types of disaster requires a multidisciplinary approach. The high percentage of maxillofacial injuries confirm that maxillofacial surgeons should form an integral part of this multidisciplinary team.
P.M. Ngumbi, L. W. Irungu, P. N. Ndegwa, N.K. Maniania. "Pathogenicity of Metarhizium anisopliae (Metch) Sorok and Beauveria bassiana (Bals) Vuill to adult Phlebotomus duboscqi (Neveu-Lemaire) in the laboratory." International Journal of Science and Nature. 2011;48:37-40. AbstractWebsite

ABSTRACT: Several strategies are employed in management of insect pests. Among these, chemical control is a priority to most farming communities where pest incidences occur while other existing options such as biological control are rarely considered. In coffee farming agro ecosystems, there are indigenous biological control agents such as the predacious phytoseiid mites, Euseius kenyae (Swirski and Ragusa) that have the potential to manage secondary pests like coffee thrips, Diarthrothrips coffeae Williams. This study was conducted to assess the population dynamics of E. kenyae and D. coffeae as well as theirinteractions under coffee agro ecosystems where various soil fertilizer sources and selective insecticides were applied as treatments. The populations of both E. kenyae and D. coffeae fluctuated during the three years study period. The E. kenyae suppressed the population of D. coffeae under various treated coffee blocks. There was negative correlation between E. kenyae and D. coffeae in year 2006 and 2008 where the increasing population of E. kenyae decreased that of D. coffeae. In year 2007, positive correlation between E. kenyae and D. coffeae was observed in some of the treatments where increased population of D. coffeae caused an increased population of E. kenyae. Euseius kenyae managed to contain the D. coffeae population to below economical injury levels (1-2 thrips per leaf) during the three years under the various coffee agro ecosystems. The use of chlorpyrifos never affected E. kenyae. Their survival and increased in number under chlorpyrifos treated coffee blocks indicated the development of resistance by the population of E. kenyae, hence the possibility of using them as a component in an Integrated Pest Management strategy in coffee.

P.M.F. M, Mbau SJ, N.J. Muthama, Inyega H, Kalai JM. "Higher Education and Skills Development in Africa: An Analytical Paper on the Role of Higher Learning Institutions on Sustainable Development. ." Journal of Sustainable Environment and Peace, . 2021;2:55-70.
P.N W, E.T.O O, A.J R. "License Plate Recognition System: Localization for Kenya.". In: Strengthening the Role of ICT in Development. Nairobi; 2010.
P.N N, J.I. K, J.N K, R.K. W. Use of Anthocyanin morphological markers to select hybrids from non-hybrids Basmati lines.; 2012. Abstract

Basmati rice (Oryza sativa L.) is preferred by consumers over other varieties because of its aroma and good cooking traits. However, its yield is genetically low compared to other pure bred lines. To increase yield of Basmati per hectare, it has become necessary to adopt hybrid rice technology that has been reported to increase yield by up to 30% above pure dwarf lines. Photoperiod-sensitive genic male sterile (PGMS) and Thermosensitive genic male sterile (TGMS) rice lines contain genes that confer male sterility under long day light-length and high temperature growth conditions, respectively. Pollination of these lines, in their male sterile period, with a viable male parent pollen produce hybrid seeds. The problem of using PGMS or TGMS is that in the tropics, day-light length is 12hours and diurnal temperature range is high, making induction of complete male-sterility in these lines difficult. The result is contamination of hybrid seeds with self-bred pure line seeds. The objective of this research work was to produce pure hybrid Basmati seeds. Hypothesis to be tested is that anthocyanin markers can be used to differentiate hybrid F1s from pure inbred seedlings. This tool can be used in selection of Basmati hybrid seedlings free from contamination with self-bred parents before transplanting and therefore save on the associated losses. The F1 seeds from a cross between PGMS or TGMS and Basmati were sown in greenhouse at KARI Mwea- Kimbibi station. Hybrid seeds were scored for anthocynanin morphological marker, by observation, to differentiate them from the pure bred lines. All hybrids involving Basmati370 and Basmati217 had very conspicuous incidence of anthocyanin which made them distinct from the parents. The conclusion is that anthocyanin can be used as a marker to separate F1 hybrid plants from the parents.

Key words: Anthocyanins, Morphological marker, Basmati, Hybrid rice seed

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