By V. Z. Gorkin
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Additional resources for Amine Oxidases in Clinical Research
Mitochondrial monoamine oxidases are intimately bound with the membrane (Gorkin, 1966) and to solubilize them requires drastic treatment of the mitochondria (Achee and coworkers, 1977). 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.
Again, in centrifuged homogenates of whole brain almost all the monoamine oxidase activity was concentrated in the mitochondrial fraction (Youdim and Holzbauer, 1976b). 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).
Although in brain tissue monoamine oxidase activity is lower than in liver and kidney, the total amount of enzyme in the central nervous system apparently exceeds what is required for the metabolism of the neurotrans mitter amines (Berrettini and coworkers, 1978). Brain tissue obtained at autopsy has been used in studies of human brain monoamine oxidase activity. Monoamine oxidases from brain tissue were remarkably stable after death, even at room temperature (Mackay and coworkers, 1978). Monoamine oxidase activity differed in different parts of the brain only between two- and four-fold (depending on the nature of the substrate used for estimating activity (Mackay and coworkers, 1978; Murphy and coworkers, 1979a).
Amine Oxidases in Clinical Research by V. Z. Gorkin