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By V. Z. Gorkin

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Unfortunately, in a review (Singer, 1974) devoted to other problems mitochondrial monoamine oxidase was quite erroneously (cf. Sawyer and Greenawalt, 1979) included in the category of so-called peripheral (in contrast to integral) proteins, loosely bound with membranes and not involved in reactions with membrane lipids. In fact, monoamine oxidases (unlike other peripheral proteins) are not solubilized by treatment of mitochondria with buffer solutions. This requires the combined effects of surface-active reagents, ultrasound and chaotropic agents.

Monoamine oxidase (substrate tyramine) of peripheral nerves is also associated with the mitochondrial fraction (Dahlström, 1972), and similarly in mouse lung (substrates serotonin and 3-phenylethylamine) ll+ (Gallagher, 1977), rat skeletal muscle (substrate C-tryptamine) (HimmsHagen and Irwin, 1976) and rat reticulocytes (substrates tryptamine and $phenylethylamine) (Quiring and Hubertus, 1977). Thrombocyte monoamine oxidase activity was detected mainly in a fraction, which, as shown by electron microscopy, contained mitochondria and their fragments (Solatunturi and Paasonen, 1966).

Among the nonionic surface-active agents, Triton X-100 is widely used for solubilizing mitochondrial monoamine oxidase. To extract the inactive proteins, bovine liver mitochondrial monoamine oxidase (substrate benzylamine) was first solubilized using Triton X-100 (Barbato and Abood, 1963). 0 for 30 min and then centrifuged (20 min at 80,000 g). 5. 0 for 30 min and centrifuged. 0 for 30 min to extract the monoamine oxidases. 0, and centrifuged again (120 min at 100,000 g). The supernatant was found to contain 40% of the monoamine oxidase activity present in the mitochondria; the specific activity of the supernatant was 4-5 times that of the mitochondria.

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