Voprosy meditsinskoi khimii (ISSN 0042-8809)

Kinetic properties of monoamine oxidase isoenzymes from the bovine brain

   
Moskvitina T.A., Kuchina N.E., Gorkin V.Z.
PubMed Id: 7179829
Year: 1982 vol: 28  issue:5  pages: 127-131
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.
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Reference: Moskvitina T.A., Kuchina N.E., Gorkin V.Z., Kinetic properties of monoamine oxidase isoenzymes from the bovine brain, Voprosy meditsinskoi khimii, 1982, vol: 28(5), 127-131.
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