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By V. Z. Gorkin

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In rat hypothalamus monoamine oxidase activity was 2 nmole of tyramine oxidized per mg protein/min (Neff and Goridis, 1972). As shown by inhibitory analysis, 55% of the total monoamine oxidase activity in rat brain is represented by type A monoamine oxidase (Neff and Goridis, 1972). However, in the brain of primates (includ­ ing man) type Β monoamine oxidases predominate (Murphy and Buchsbaum, 1978). Less than 10% of the total monoamine oxidase activity (substrate tryptamine) of the human brain is found in neurons (Adolfsson and coworkers, 1978).

All three forms of amine oxidase are localized not in nerve terminals but in endothelial cells lining blood vessels in lung tissue (Roth and Gillis, 1975a; Roth and Venter, 1978). In rat lung A and Β monoamine oxidases were found ( A : B = 5 5 : 5 4 ) , but the amine 28 Amine Oxidases: Clinical Aspects oxidase that is inhibited by semicarbazide was absent (Kung and Wilson, 1979). 1 1 + CMonoamine oxidase activity has been detected in mouse skin (substrate ll+ llt tyramine or C-serotonin) (Essman, 1977).

04 nmole oxidized kynuramine per mg protein/min (Dial and Clarke, 1977). This was approxi­ mately four times the monoamine oxidase activity estimated under similar conditions in the aorta and the inferior vena cava of rats. No amine oxidase from human venous tissues was resistant to the inhibitory effect of clorgyline and sensitive to the effect of semicarbazide. 5 nmole ß-phenylethylamine oxidized per mg protein/min) (Fuentes and Neff, 1977). Rabbit lung monoamine oxidase activity (substrates serotonin and 3-phenylethylamine) has been shown by inhibitor analysis to result from the presence of three forms of amine oxidase.

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