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Some kinetic properties of guinea pig liver monoamine oxidase

  • C. J. Barwell
  • S. A. Ebrahimi
Conference paper
Part of the Journal of Neural Transmission book series (NEURAL SUPPL, volume 41)

Summary

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.

Keywords

Monoamine Oxidase Liver Mitochondrion Selective Substrate Monoamine Oxidase Activity Inhibitor Sensitivity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • C. J. Barwell
    • 1
  • S. A. Ebrahimi
    • 1
  1. 1.School of Pharmacy and Biomedical SciencesUniversity of PortsmouthPortsmouthUK

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