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The oxidation of dopamine and epinine by the two forms of monoamine oxidase from rat liver

  • M. Strolin Benedetti
  • G. Sanson
  • L. Bona
  • M. Gallina
  • S. Persiani
  • K. F. Tipton
Part of the Journal of Neural Transmission. Supplement book series (NEURAL SUPPL, volume 52)

Summary

Information on the “in vitro” oxidation of epinine by monoamine oxidase (MAO) compared to dopamine is very poor. The aim of this work was to study the oxidative deamination of epinine and dopamine by rat liver MAO-A and MAO-B.

The contributions of MAO-A and B to the metabolism of dopamine (55% and 45%, respectively) and epinine (70% and 30%, respectively) were similar. The results of this study show that epinine is a substrate for both forms of MAO in rat liver, although the contribution of MAO A to the deamination of this secondary amine appears to be slightly more important than that of MAO B.

Keywords

Monoamine Oxidase Secondary Amine Liver Homogenate Oxidative Deamination Dihydroxyphenylacetic Acid 
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 Wien 1998

Authors and Affiliations

  • M. Strolin Benedetti
    • 1
    • 1
  • G. Sanson
    • 1
  • L. Bona
    • 1
  • M. Gallina
    • 1
  • S. Persiani
    • 1
  • K. F. Tipton
    • 2
  1. 1.Preclinical Development and Human PharmacologyZambon Group S.p.A.BressoItaly
  2. 2.Department of BiochemistryTrinity CollegeDublinIreland

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