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Separation of two monoamine oxidases from bovine bran

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Summary

  1. 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. 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. 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. 4.

    Some of the physiological implications of these findings are discussed.

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Author notes

  1. Roy McCauley

    Present address: Department of Pharmacology, Downstate Medical Center, State University of New York, Brooklyn, New York, USA

Authors and Affiliations

  1. Section of Biochemistry and Molecular Biology, Cornell University, 14850, Ithaca, New York, USA

    Roy McCauley & Efraim Racker

Authors
  1. Roy McCauley
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  2. Efraim Racker
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Additional information

This work was supported by United States Public Health Service Postdoctoral Fellowship Award 2 FO2 NS47108-02 from the National Institute of Neurological Diseases and Stroke.

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McCauley, R., Racker, E. Separation of two monoamine oxidases from bovine bran. Mol Cell Biochem 1, 73–81 (1973). https://doi.org/10.1007/BF01659940

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