title: [Kinetic properties of monoamine oxidase isoenzymes from the bovine brain].
abstract: Multiple forms of monoamine oxidase (MAO I, IIa, IIb, III) from bovine brain, separated by means of affinity chromatography on AH-Sepharose 4B, were dissimilar in kinetics of deamination of serotonin and beta-phenylethylamine used as substrates of the MAO of A and B types. MAO-I catalyzed the deamination of beta-phenyl ethylamine and serotonin. Km and Vmax values could not be calculated for MAO-IIa since the rate of enzymatic reactions was characterized by a complicated dependence on concentration of serotonin in a sample. MAO-IIb catalyzed also the deamination of both AMO substrates.
mesh_terms: D015078:2-Hydroxyphenethylamine / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D003641:Deamination; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008995:Monoamine Oxidase / Q000378:metabolism*; D012701:Serotonin / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D012701:Serotonin; D015078:2-Hydroxyphenethylamine; D008995:Monoamine Oxidase
vernacular_title: Kineticheskie svoĭstva mnozhestvennykh form monoaminoksidazy mozga byka.