Abstract

1. Two forms of monoamine oxidase have been separated from bovine brain mitochondria. The two enzymes differ in substrate specificity, sensitivity to inhibitors and are immunologically distinct. 2. Monoamine oxidase A does not cross-react with an antibody against bovine liver monoamine oxidase. It catalyzes the oxidation of tyramine, tryptamine and the biogenic amines norepinephrine, serotonin and dopamine. Benzylamine is very slowly oxidized. Harmaline inhibits the enzyme at 10−7 M concentration, amphetamine at 10−4 M. 3. Monoamine oxidase B is precipitated by an antibody against bovine liver monoamine oxidase but the precipitate is enzymatically active. The enzyme catalyzes the oxidation of benzylamine as well as tyramine, tryptamine and dopamine, whereas little or no activity was found with norepinephrine, or serotonin, as substrates. The enzyme is inhibited by pargyline and is relatively insensitive to harmaline. 4. Some of the physiological implications of these findings are discussed.

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