Some kinetic properties of guinea pig liver monoamine oxidase

Barwell, C.J. and Ebrahimi, S.A. (1994) Some kinetic properties of guinea pig liver monoamine oxidase. Journal of Neural Transmission, Supplement (41). pp. 41-45.

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Titration of monoamine oxidase activity in isolated guinea pig liver mitochondria with clorgyline and assay of remaining activity with tyramine yielded biphasic inhibition curves. The position of the plateaus obtained with mitochondria from four animals, indicated that the B form of monoamine oxidase accounted for 30 to 70 of the tyramine deaminating activity. Benzylamine deamination was selectively inhibited by (-)-deprenyl. However, benzylamine and other amines which are selective substrates for the B form of monoamine oxidase from the rat, were deaminated at only low rates by the guinea pig liver enzyme. Guinea pig liver contains a monoamine oxidase-B which is unusual in that although it exhibits apparently normal sensitivity to selective irreversible inhibitors, it has a low catalytic activity with substrates which the enzyme from rat liver deaminates rapidly.

Item Type: Article
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Uncontrolled Keywords: amine oxidase (flavin containing) isoenzyme b; clorgyline; monoamine oxidase inhibitor; selegiline; tyramine; amine oxidase (flavin containing); benzylamine; benzylamine derivative, animal tissue; conference paper; controlled study; enzyme kinetics; guinea pig; liver; male; nonhuman; priority journal; rat; animal; article; deamination; drug effect; enzymology; kinetics; liver mitochondrion; metabolism; rat strain, Animal; Benzylamines; Clorgyline; Deamination; Guinea Pigs; Kinetics; Liver; Male; Mitochondria, Liver; Monoamine Oxidase; Rats; Rats, Wistar; Support, Non-U.S. Gov't; Tyramine
Depositing User: EPrints System Admin
Date Deposited: 19 Jul 2017 10:13
Last Modified: 19 Jul 2017 10:13

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