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Deamination of 5‐Hydroxytryptamine by Both Forms of Monoamine Oxidase in the Rat Brain
Author(s) -
Fowler Christopher J.,
Tipton Keith F.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb08692.x
Subject(s) - clorgyline , monoamine oxidase , monoamine oxidase b , phenethylamine , monoamine oxidase a , serotonin , selegiline , monoamine neurotransmitter , chemistry , oxidative deamination , in vitro , deamination , pharmacology , biochemistry , enzyme , stereochemistry , medicine , biology , receptor , disease , parkinson's disease
Km and V max values of monoamine oxidase (MAO) A and B towards 5‐hydroxytryptamine were determined for rat brain homogenates after the in vitro inhibition of one of the two forms by the selective inhibitors clorgyline and l ‐deprenyl. K m values of 178 and 1170μ m , and V max values of 0.73 and 0.09 nmol·mg protein −1 ·min −1 towards 5‐hydroxytryptamine were found for MAO‐A and ‐B, respectively. The K 1 for 5‐hydroxytryptamine as a competitive inhibitor of β‐phenethylamine oxidation by MAO‐B was found to be 1400 μm. The significance of these findings is discussed.