Bio

DR. MBUGUA PAUL MUNGAI

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Publications


2012

Yenesew, A, KARIUKI HELLENN, Patel NB, Mbugua PM, Kanui TI.  2012.  Antinocieptive activity of Toddalia asiatica (L) Lam. in models of central and peripheral pain.

2011

2006

MUNGAI, DRMBUGUAPAUL.  2006.  Mbaabu Mathiu; P.M. Mbugua and J. Mugweru (2006): Screening for biological activity of Solanum Incanum and Conyza Sumatrensis using the isolated rabbit intestine The Veterinarian (in press).. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
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1988

MUNGAI, DRMBUGUAPAUL.  1988.  Mbugua P M Welder A A and Acosta D (1988): Cardiotoxicity of Kenyan green mamba (Dendroaspis angusticeps) venom and its fractionated components in primary cultures of rat myocardial cells. Toxicology 52 : 187. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712. The cardiotoxic actions of Kenyan green mamba (Dendroaspis angusticeps) venom have been investigated using primary myocardial cell cultures isolated from neonatal rat hearts. The cardiotoxic actions of the whole venom and its fractionated components were evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, decreases in viability and inhibition of spontaneous beating activity. The whole venom caused time- and concentration-dependent arrest of myocardial contraction, leakage of LDH, extensive disruption of cell monolayer, and decreases in viability. The venom was separated into 6 (DaI to DaVI) fractions by gel permeation chromatography on Sephadex G-50. Spontaneous beating activity was abolished by DaI to DaVI at high concentrations, while at lower doses they induced progressive depression of beating frequency after a 3-h treatment period. DaI to DaIV caused significant leakage of LDH, morphological damage, and decreases in viability after a 6-h incubation period. The most cardiotoxic fraction (DaIV), which also contains about 54% of the total protein of the whole venom, was fractionated into 18 polypeptides (Da1 to Da18) by ion exchange chromatography on Bio-Rex 70. On the basis of their ability to abolish myocardial contractility, release LDH, alter cellular structure, lyse cell membranes and reduce viability, the 18 fractions have been divided into 4 arbitrary subgroups of cytotoxins: cardiotoxins, Da1 to Da3; cardiotoxin-like polypeptides, Da4 to Da12, Da14; less active membrane lytic polypeptides, Da13, Da15 to Da17; and membrane lytic polypeptide, Da18. Marked synergistic cell membrane lysis occurred in myocardial cell cultures treated simultaneously with 2 cardiotoxin-like polypeptides, Da7 and Da11. It is suggested that the additive and synergistic cardiotoxic effects of high molecular weight cytotoxic proteins (DaI to DaIII), very low molecular weight cholinomimetic substances (DaV to DaVI) and the 4 subgroups of cardiotoxins may directly contribute to the pronounced cardiovascular problems observed in victims of green mamba bites. PMID: 3188032 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1988.  Mbugua P M Welder A A and Acosta D (1988): Cardiotoxicity of Jamesoni's mamba (Dendroaspis jamesoni) venom and its fractionated components in primary cultures of rat myocardial cells. In vitro cell & Dev. Biol. 24 (8): 743. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract

Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712.

Primary cultures of spontaneously beating myocardial cells isolated from neonatal rat hearts were used to screen the cardiotoxic effects of Jamesoni's mamba (Dendroaspis jamesoni) venom and components isolated from the venom by gel filtration and ion exchange chromatography. Cardiotoxicity was evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, cellular viability, and alterations in spontaneous beating activity. The whole venom caused dose- and time-dependent leakage of LDH, disruption of the cell monolayer, decreases in viability, and inhibition of beating activity. Gel filtration of the venom yielded eight fractions (DjI to DjVIII). DjI (30 micrograms/ml), DjII (20 micrograms/ml), and DjV (20 micrograms/ml) caused significant (P less than 0.001) leakage of LDH, extensive morphologic damage, and decreases in viability. At lower concentrations DjI to DjVIII caused progressive inhibition of spontaneous beating activity. The main fraction (DjV), which was the most toxic, was further separated into 14 polypeptides (Dj1 to Dj14) by ion-exchange chromatography using Bio-Rex 70. Based on the ability to induce LDH leakage, produce morphologic damage, lyse cell membranes, and arrest beating activity, four categories of polypeptides were identified: cardiotoxins, Dj1 and Dj2; cardiotoxinlike polypeptides, Dj3 to Dj8; less active membrane lytic polypeptides, Dj9 to Dj13; and membrane lytic polypeptide, Dj14.

PMID: 3410805 [PubMed - indexed for MEDLINE]

MUNGAI, DRMBUGUAPAUL.  1988.  Mbugua P M Welder A A and Acosta D (1988): Isolation and characterization of four subgroups of mamba ( Dendroaspis ) cardiotoxins using primary cultures of rat myocardial cells. The Toxicologist 8: 159. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
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MUNGAI, DRMBUGUAPAUL.  1988.  Adem A Asblom A Johansson G Mbugua P M and Karlsson E (1988): Toxins from the venom of the green mamba Dendroaspis angusticeps that inhibit the binding of quinuclidinyl benzilate to muscarinic acetylcholine receptors (BBA 12211). Biochim Biophys Acta 968 . Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract

Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712.

Primary cultures of spontaneously beating myocardial cells isolated from neonatal rat hearts were used to screen the cardiotoxic effects of Jamesoni's mamba (Dendroaspis jamesoni) venom and components isolated from the venom by gel filtration and ion exchange chromatography. Cardiotoxicity was evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, cellular viability, and alterations in spontaneous beating activity. The whole venom caused dose- and time-dependent leakage of LDH, disruption of the cell monolayer, decreases in viability, and inhibition of beating activity. Gel filtration of the venom yielded eight fractions (DjI to DjVIII). DjI (30 micrograms/ml), DjII (20 micrograms/ml), and DjV (20 micrograms/ml) caused significant (P less than 0.001) leakage of LDH, extensive morphologic damage, and decreases in viability. At lower concentrations DjI to DjVIII caused progressive inhibition of spontaneous beating activity. The main fraction (DjV), which was the most toxic, was further separated into 14 polypeptides (Dj1 to Dj14) by ion-exchange chromatography using Bio-Rex 70. Based on the ability to induce LDH leakage, produce morphologic damage, lyse cell membranes, and arrest beating activity, four categories of polypeptides were identified: cardiotoxins, Dj1 and Dj2; cardiotoxinlike polypeptides, Dj3 to Dj8; less active membrane lytic polypeptides, Dj9 to Dj13; and membrane lytic polypeptide, Dj14.

PMID: 3410805 [PubMed - indexed for MEDLINE]

1987

MUNGAI, DRMBUGUAPAUL.  1987.  Davilla J Mbugua P M and Acosta D (1987): Cytotoxic actions of Dendroaspis venoms in primary cultures of rat hepatocytes. Tissue Culture Ass. Manual 38 : 74. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712. The cardiotoxic actions of Kenyan green mamba (Dendroaspis angusticeps) venom have been investigated using primary myocardial cell cultures isolated from neonatal rat hearts. The cardiotoxic actions of the whole venom and its fractionated components were evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, decreases in viability and inhibition of spontaneous beating activity. The whole venom caused time- and concentration-dependent arrest of myocardial contraction, leakage of LDH, extensive disruption of cell monolayer, and decreases in viability. The venom was separated into 6 (DaI to DaVI) fractions by gel permeation chromatography on Sephadex G-50. Spontaneous beating activity was abolished by DaI to DaVI at high concentrations, while at lower doses they induced progressive depression of beating frequency after a 3-h treatment period. DaI to DaIV caused significant leakage of LDH, morphological damage, and decreases in viability after a 6-h incubation period. The most cardiotoxic fraction (DaIV), which also contains about 54% of the total protein of the whole venom, was fractionated into 18 polypeptides (Da1 to Da18) by ion exchange chromatography on Bio-Rex 70. On the basis of their ability to abolish myocardial contractility, release LDH, alter cellular structure, lyse cell membranes and reduce viability, the 18 fractions have been divided into 4 arbitrary subgroups of cytotoxins: cardiotoxins, Da1 to Da3; cardiotoxin-like polypeptides, Da4 to Da12, Da14; less active membrane lytic polypeptides, Da13, Da15 to Da17; and membrane lytic polypeptide, Da18. Marked synergistic cell membrane lysis occurred in myocardial cell cultures treated simultaneously with 2 cardiotoxin-like polypeptides, Da7 and Da11. It is suggested that the additive and synergistic cardiotoxic effects of high molecular weight cytotoxic proteins (DaI to DaIII), very low molecular weight cholinomimetic substances (DaV to DaVI) and the 4 subgroups of cardiotoxins may directly contribute to the pronounced cardiovascular problems observed in victims of green mamba bites. PMID: 3188032 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1987.  Mbugua P M Welder A. A and Acosta D (1987): The toxic effects of mamba snake venoms in primary endothelial cell cultures. The Toxicologist 7 : 92. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712. The cardiotoxic actions of Kenyan green mamba (Dendroaspis angusticeps) venom have been investigated using primary myocardial cell cultures isolated from neonatal rat hearts. The cardiotoxic actions of the whole venom and its fractionated components were evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, decreases in viability and inhibition of spontaneous beating activity. The whole venom caused time- and concentration-dependent arrest of myocardial contraction, leakage of LDH, extensive disruption of cell monolayer, and decreases in viability. The venom was separated into 6 (DaI to DaVI) fractions by gel permeation chromatography on Sephadex G-50. Spontaneous beating activity was abolished by DaI to DaVI at high concentrations, while at lower doses they induced progressive depression of beating frequency after a 3-h treatment period. DaI to DaIV caused significant leakage of LDH, morphological damage, and decreases in viability after a 6-h incubation period. The most cardiotoxic fraction (DaIV), which also contains about 54% of the total protein of the whole venom, was fractionated into 18 polypeptides (Da1 to Da18) by ion exchange chromatography on Bio-Rex 70. On the basis of their ability to abolish myocardial contractility, release LDH, alter cellular structure, lyse cell membranes and reduce viability, the 18 fractions have been divided into 4 arbitrary subgroups of cytotoxins: cardiotoxins, Da1 to Da3; cardiotoxin-like polypeptides, Da4 to Da12, Da14; less active membrane lytic polypeptides, Da13, Da15 to Da17; and membrane lytic polypeptide, Da18. Marked synergistic cell membrane lysis occurred in myocardial cell cultures treated simultaneously with 2 cardiotoxin-like polypeptides, Da7 and Da11. It is suggested that the additive and synergistic cardiotoxic effects of high molecular weight cytotoxic proteins (DaI to DaIII), very low molecular weight cholinomimetic substances (DaV to DaVI) and the 4 subgroups of cardiotoxins may directly contribute to the pronounced cardiovascular problems observed in victims of green mamba bites. PMID: 3188032 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1987.  Swann J Mbugua P M and Acosta D (1987): Nephrotoxicity induced by mamba venoms in cultured rat cortical epithelial cells. Tissue Culture Ass. Manual 38 : 72. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712. The cardiotoxic actions of Kenyan green mamba (Dendroaspis angusticeps) venom have been investigated using primary myocardial cell cultures isolated from neonatal rat hearts. The cardiotoxic actions of the whole venom and its fractionated components were evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, decreases in viability and inhibition of spontaneous beating activity. The whole venom caused time- and concentration-dependent arrest of myocardial contraction, leakage of LDH, extensive disruption of cell monolayer, and decreases in viability. The venom was separated into 6 (DaI to DaVI) fractions by gel permeation chromatography on Sephadex G-50. Spontaneous beating activity was abolished by DaI to DaVI at high concentrations, while at lower doses they induced progressive depression of beating frequency after a 3-h treatment period. DaI to DaIV caused significant leakage of LDH, morphological damage, and decreases in viability after a 6-h incubation period. The most cardiotoxic fraction (DaIV), which also contains about 54% of the total protein of the whole venom, was fractionated into 18 polypeptides (Da1 to Da18) by ion exchange chromatography on Bio-Rex 70. On the basis of their ability to abolish myocardial contractility, release LDH, alter cellular structure, lyse cell membranes and reduce viability, the 18 fractions have been divided into 4 arbitrary subgroups of cytotoxins: cardiotoxins, Da1 to Da3; cardiotoxin-like polypeptides, Da4 to Da12, Da14; less active membrane lytic polypeptides, Da13, Da15 to Da17; and membrane lytic polypeptide, Da18. Marked synergistic cell membrane lysis occurred in myocardial cell cultures treated simultaneously with 2 cardiotoxin-like polypeptides, Da7 and Da11. It is suggested that the additive and synergistic cardiotoxic effects of high molecular weight cytotoxic proteins (DaI to DaIII), very low molecular weight cholinomimetic substances (DaV to DaVI) and the 4 subgroups of cardiotoxins may directly contribute to the pronounced cardiovascular problems observed in victims of green mamba bites. PMID: 3188032 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1987.  Mbugua P M Welder A A and Acosta D (1987): The toxic effects of mamba snake venoms in primary myocardial cell cultures. The Toxicologist 7: 92. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Department of Pharmacology and Toxicology, College of Pharmacy, University of Texas, Austin 78712. The cardiotoxic actions of Kenyan green mamba (Dendroaspis angusticeps) venom have been investigated using primary myocardial cell cultures isolated from neonatal rat hearts. The cardiotoxic actions of the whole venom and its fractionated components were evaluated on the basis of leakage of lactate dehydrogenase (LDH), changes in morphology, cell membrane lysis, decreases in viability and inhibition of spontaneous beating activity. The whole venom caused time- and concentration-dependent arrest of myocardial contraction, leakage of LDH, extensive disruption of cell monolayer, and decreases in viability. The venom was separated into 6 (DaI to DaVI) fractions by gel permeation chromatography on Sephadex G-50. Spontaneous beating activity was abolished by DaI to DaVI at high concentrations, while at lower doses they induced progressive depression of beating frequency after a 3-h treatment period. DaI to DaIV caused significant leakage of LDH, morphological damage, and decreases in viability after a 6-h incubation period. The most cardiotoxic fraction (DaIV), which also contains about 54% of the total protein of the whole venom, was fractionated into 18 polypeptides (Da1 to Da18) by ion exchange chromatography on Bio-Rex 70. On the basis of their ability to abolish myocardial contractility, release LDH, alter cellular structure, lyse cell membranes and reduce viability, the 18 fractions have been divided into 4 arbitrary subgroups of cytotoxins: cardiotoxins, Da1 to Da3; cardiotoxin-like polypeptides, Da4 to Da12, Da14; less active membrane lytic polypeptides, Da13, Da15 to Da17; and membrane lytic polypeptide, Da18. Marked synergistic cell membrane lysis occurred in myocardial cell cultures treated simultaneously with 2 cardiotoxin-like polypeptides, Da7 and Da11. It is suggested that the additive and synergistic cardiotoxic effects of high molecular weight cytotoxic proteins (DaI to DaIII), very low molecular weight cholinomimetic substances (DaV to DaVI) and the 4 subgroups of cardiotoxins may directly contribute to the pronounced cardiovascular problems observed in victims of green mamba bites. PMID: 3188032 [PubMed - indexed for MEDLINE]

1985

MUNGAI, DRMBUGUAPAUL.  1985.  Mbugua P M and Karlsson (1985): Fasciculins from Dendroaspis angusticeps venom and their effects on cholinesterases. Toxicon 23 : 595.. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Anderson AJ, Harvey AL, Mbugua PM. Fasciculin 2, a polypeptide from green mamba (Dendroaspis angusticeps) venom, causes an increase in the twitch response of mouse phrenic nerve-hemidiaphragm preparations to indirect stimulation. Intracellular recording reveals that fasciculin 2 augments neuromuscular transmission by increasing the amplitude and duration of endplate potentials. Its action is not reversed by washing. Interactions with neostigmine confirm that fasciculin 2 acts as an anticholinesterase. It has no presynaptic actions on transmitter release or postsynaptic receptor blocking actions. On chicken muscle preparations, fasciculin 2 has no anticholinesterase actions. Because of this selectivity and its apparent irreversibility, fasciculin 2 should be useful in characterizing different forms of acetylcholinesterase. PMID: 2986055 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1985.  Mbugua P M (1985): Anticholinesterase toxins in mamba venoms. PhD Thesis, University of Nairobi. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Anderson AJ, Harvey AL, Mbugua PM. Fasciculin 2, a polypeptide from green mamba (Dendroaspis angusticeps) venom, causes an increase in the twitch response of mouse phrenic nerve-hemidiaphragm preparations to indirect stimulation. Intracellular recording reveals that fasciculin 2 augments neuromuscular transmission by increasing the amplitude and duration of endplate potentials. Its action is not reversed by washing. Interactions with neostigmine confirm that fasciculin 2 acts as an anticholinesterase. It has no presynaptic actions on transmitter release or postsynaptic receptor blocking actions. On chicken muscle preparations, fasciculin 2 has no anticholinesterase actions. Because of this selectivity and its apparent irreversibility, fasciculin 2 should be useful in characterizing different forms of acetylcholinesterase. PMID: 2986055 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1985.  Ndungu T K Kofi-Tsekpo W M and Mbugua P M (1985): Irradiation sterilization of pharmaceuticals and other medicinal products: Methods and approach for Kenya Proc. 6 th Ann. Med. Sci. Conf., KEMRI/KETRI .. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Anderson AJ, Harvey AL, Mbugua PM. Fasciculin 2, a polypeptide from green mamba (Dendroaspis angusticeps) venom, causes an increase in the twitch response of mouse phrenic nerve-hemidiaphragm preparations to indirect stimulation. Intracellular recording reveals that fasciculin 2 augments neuromuscular transmission by increasing the amplitude and duration of endplate potentials. Its action is not reversed by washing. Interactions with neostigmine confirm that fasciculin 2 acts as an anticholinesterase. It has no presynaptic actions on transmitter release or postsynaptic receptor blocking actions. On chicken muscle preparations, fasciculin 2 has no anticholinesterase actions. Because of this selectivity and its apparent irreversibility, fasciculin 2 should be useful in characterizing different forms of acetylcholinesterase. PMID: 2986055 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1985.  Karlsson E Mbugua P M and Rodriguez-Ithurralde D (1985): Anticholinesterase toxins. Pharm. Ther. 30 : 259. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Anderson AJ, Harvey AL, Mbugua PM. Fasciculin 2, a polypeptide from green mamba (Dendroaspis angusticeps) venom, causes an increase in the twitch response of mouse phrenic nerve-hemidiaphragm preparations to indirect stimulation. Intracellular recording reveals that fasciculin 2 augments neuromuscular transmission by increasing the amplitude and duration of endplate potentials. Its action is not reversed by washing. Interactions with neostigmine confirm that fasciculin 2 acts as an anticholinesterase. It has no presynaptic actions on transmitter release or postsynaptic receptor blocking actions. On chicken muscle preparations, fasciculin 2 has no anticholinesterase actions. Because of this selectivity and its apparent irreversibility, fasciculin 2 should be useful in characterizing different forms of acetylcholinesterase. PMID: 2986055 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1985.  Anderson A J Harvey A L and Mbugua P M (1985): Effects of fasciculin 2, an anticholinesterase polypeptide from green mamba venom, on neuromuscular transmission in mouse diaphragm preparations Neurosci. Lett. 54: 123.. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Anderson AJ, Harvey AL, Mbugua PM. Fasciculin 2, a polypeptide from green mamba (Dendroaspis angusticeps) venom, causes an increase in the twitch response of mouse phrenic nerve-hemidiaphragm preparations to indirect stimulation. Intracellular recording reveals that fasciculin 2 augments neuromuscular transmission by increasing the amplitude and duration of endplate potentials. Its action is not reversed by washing. Interactions with neostigmine confirm that fasciculin 2 acts as an anticholinesterase. It has no presynaptic actions on transmitter release or postsynaptic receptor blocking actions. On chicken muscle preparations, fasciculin 2 has no anticholinesterase actions. Because of this selectivity and its apparent irreversibility, fasciculin 2 should be useful in characterizing different forms of acetylcholinesterase. PMID: 2986055 [PubMed - indexed for MEDLINE]

1984

MUNGAI, DRMBUGUAPAUL.  1984.  Karlsson E and Mbugua P M (1984): A comparison of gel filtration, ion-exchange, hydrophobic interaction and reverse phase chromatography in the fractionation of complex samples LKB Appl. Note 354.. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1984.  Karlsson E and Mbugua P M (1984): Further purification of some anticholinesterases in black mamba venom using HPLC. LKB Appl. Note 355. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1984.  Karlsson E and Mbugua P M (1984): Isolation of anticholinesterase toxins in snake venoms LKB Appl. Note 353.. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1984.  Karlsson E Mbugua P M and Rodriguez-Ithurralde D (1984): Fasculins, anticholinesterase toxins from the venom of the green mamba, Dendroaspis angusticeps J. Physiol., Paris 79 232. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]
MUNGAI, DRMBUGUAPAUL.  1984.  Harvey A L Anderson A J Mbugua P M and Karlsson E (1984): Toxins from mamba venoms that facilitate neuromuscular transmission J. Toxicol-Toxins Review 3 (2 & 3) 91. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]

1983

MUNGAI, DRMBUGUAPAUL.  1983.  Thairu K Wasunna A Kofi-Tsekpo W M and Mbugua P M (1983): Chemical and Pharmacological examination of the herbal preparation . Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract
Two toxins that are potent inhibitors of acetylcholinesterase have been isolated from the venom of the green mamba, Dendroaspis angusticeps. The toxins have been called fasciculins since after injection into mice (i.p. 0.5-3 micrograms/g body weight) they cause severe, generalized and long-lasting (5-7 h) fasciculations. Homogenates of diaphragm, tibialis anterior and gastrocnemius muscles from mice injected with fasciculins showed a decrease in acetylcholinesterase activity by 45-60% compared to muscles from control animals. Histochemical staining revealed a greatly reduced acetylcholinesterase activity at neuromuscular junctions. Fasciculins have 61 amino acid residues and four disulfides. The molecular weights are 6765 (fasciculin 1) and 6735 (fasciculin 2). The sequences of the two toxins differ probably only at one position by a replacement of Tyr with Asp/Asn. 1 g of venom contained about 40 mg of fasciculins, 2/3 of which was fasciculin 2. A similar inhibitor has also been isolated from D. polylepis (black mamba) venom. The sequence of fasciculin 2 is known. Most of the positive charges are concentrated in a small section of the central part of the molecule, and most of the negative charges are in the C-terminal region. Fasciculins appear to have a pronounced dipole character. Fasciculin binds to the peripheral anionic site, since it can displace propidium, a probe for that site, from acetylcholinesterase. In vitro, in Krebs-Henseleit solution containing 2 mM NaH2PO4 (pH 7.4), fasciculin 2 inhibits acetylcholinesterase from human erythrocytes (Ki = 1.1 X 10(-10) M, 37 degrees C), rat muscle (Ki = 1.2 X 10(-10) M, 37 degrees C) and Electrophorus electricus (Ki = 3.0 X 10(-10) M, 22 degrees C).(ABSTRACT TRUNCATED AT 250 WORDS) PMID: 6530667 [PubMed - indexed for MEDLINE]

1982

MUNGAI, DRMBUGUAPAUL.  1982.  Mbugua P M Thairu K and Telang B V (1982): Neuropharmacological studies of certain snake venoms Indian J Pharmacol 14: 115-. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract

Mbugua PM, Thairu K, Ng'ang'a JN, Telang BV.

A cholinomimetic substance was isolated from desiccated venom of Dendroaspis polylepis by one-dimensional ascending paper chromatography. The migratory and staining properties of the substance were compared with those of standard acetylcholine. Pharmacological and biochemical identification was carried out on various in vitro and in vivo biological test objects as well as with high-voltage paper electrophoresis. The assay of the cholinomimetic substance was done on both superfused guinea pig ileum and hamster stomach strips. The cholinomimetic substance content was 2.44 - 3.46mg/0.96gm of total protein in the desiccated venom.

PMID: 7100627 [PubMed - indexed for MEDLINE]

MUNGAI, DRMBUGUAPAUL.  1982.  Mbugua P M Thairu K and Telang B V (1982): Identification and estimation of a cholinomimetic substance in the venom of Dendroaspis polylepis Res. Commun. Chem. Pathol. Pharmacol. 36: 187-. Federation of Analytical Chemistry and Spectroscopy Society (FACSS) XV, Boston, November 1988. : AWC and FES Abstract

Mbugua PM, Thairu K, Ng'ang'a JN, Telang BV.

A cholinomimetic substance was isolated from desiccated venom of Dendroaspis polylepis by one-dimensional ascending paper chromatography. The migratory and staining properties of the substance were compared with those of standard acetylcholine. Pharmacological and biochemical identification was carried out on various in vitro and in vivo biological test objects as well as with high-voltage paper electrophoresis. The assay of the cholinomimetic substance was done on both superfused guinea pig ileum and hamster stomach strips. The cholinomimetic substance content was 2.44 - 3.46mg/0.96gm of total protein in the desiccated venom.

PMID: 7100627 [PubMed - indexed for MEDLINE]

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