Bio

DR. VINCENT OCHIENG ODUOL BIO

Academic Qualifications:

Bsc. University of Nairobi Msc. University of Nairobi

PhD. University of Nairobi

Extra Responsibilities:

Member of College Healthy Safety Committee, Class

Coordinator Bsc. III, Department of Biochemistry Exam

Officer, Member of Department of Biochem SYCA.

Review Committee, Member of College Brochure

Committee

AREAS OF SPECIALIZATION

Biochemistry (Protein/ Molecular Biology)

RESEARCH INTERESTS

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Publications


1996

ODUOL, DROCHIENGVINCENT.  1996.  Ochanda JO, Mumcuoglu KY, Ben-Yakir D, Okuru JK, Oduol VO, Galun R.Characterization of body louse midgut proteins recognized by resistant hosts.Med Vet Entomol. 1996 Jan;10(1):35-8.. Med Vet Entomol. 1996 Jan;10(1):35-8.. : Kireti VM, Atinga JEO Abstract
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.
ODUOL, DROCHIENGVINCENT.  1996.  Ochanda, J.O., Momcuoglu, K.Y., Ben-Yakir, D., Okuru, J.K., Oduol, V.O., and Galun, R., (1996). Characterization of body louse Pediculus humanus humanus mid gut proteins recognized by resistant hosts. Medical and Veterinary Entomology 10, 35-38.. Medical and Veterinary Entomology 10, 35-38.. : Kireti VM, Atinga JEO Abstract
BackgroundOsgood-Schlatter disease is a common cause of anterior knee pain inthe adolescent. Treatment is usually conservative with surgery reservedfor those who do not respond to this treatment. There is little publishedwork regarding the experience with the disease in our local set up. This series documents the experience with 35 adolescents treated for the disease.DesignCase seriesSubjectsThirty five adolescents with clinical and radiological diagnoses ofOsgood-Schlatter disease at Nairobi and Kenyatta National Hospitals,between 2001and 2007.MethodPatients were evaluated for demographics, knee involvement, activitiesassociated with pain and treatment outcomeResultsThere were 28 males and 7 females, aged 10 to 16 years (mean 12.8years). Thirteen had bilateral knee involvement. Twenty two were involved in active sports while the rest had constant pain and unable to sit or kneel. A family history of the disease was documented in one case.Thirty adolescents responded well to the conservative treatment. Inthe five adolescents who underwent surgery, the patella tendon wasedematous with thickening of the tendon sheath and neovascularisation.All the operated adolescents returned to active sports with 6 weeks after the surgery.ConclusionOsgood-Schlatter disease is a self-limiting condition in majority ofadolescents. Surgery when indicated has an excellent outcome.

1993

ODUOL, DROCHIENGVINCENT.  1993.  Ochieng, V.O., Osir, E.O., Ochanda, J.O., and Olembo, N. K. (1993). Temporal synthesis of cuticle proteins during development in Glossina morsitans. Comparative Biochemistry and Physiology 105B(2), 309-316.. Comparative Biochemistry and Physiology 105B(2), 309-316.. : Kireti VM, Atinga JEO Abstract
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.
ODUOL, DROCHIENGVINCENT.  1993.  Olembo, N.K., Nguu, E.K., Ochanda, J.O. and Ochieng, V.O. (1993). Inhibition of blood meal digestion in tsetse fly Glossina morsitans centralis fed on rabbits immunized with tsetse mid gut proteins. East African Medical Journal; 71. 651-655.. East African Medical Journal; 71. 651-655.. : Kireti VM, Atinga JEO Abstract
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 117 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.

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