Abstract
Abstract Incubation of highly purified monoamine oxidase (monoamine:O2-oxidoreductase (deaminating) EC 1.4.3.4) from bovine liver mitochondria in the presence of oxidized oleic acid caused a reversible decrease in the content of —SH groups of the enzyme preparations, which was probably due to partial oxidation of the —SH groups. Treatment of highly purified monoamine oxidase with some oxidizing agents not only decreased the rate of deamination of monoamines but also induced the appearance of a new property that was not exhibited by the untreated monoamine oxidase; namely, an ability to catalyze deamination of histamine, diamines, and some other nitrogenous compounds. The induced reactions were inhibited by carbonyl reagents but not by monoamine oxidase inhibitors. Treatment with reducing agents eliminated the effects of oxidized oleic acid on the catalytic properties of highly purified mitochondrial monoamine oxidase and partially restored the content of —SH groups. The data obtained are in agreement with the results of studies on the effects of oxidizing agents on monoamine oxidase activity of mitochondria.
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