Isolation and Characterization of Soluble Monoamine Oxidase
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Monoamine oxidase (MAO) catalyzes the oxidative deamination of the monoamines including many amines of natural origin. The majority of MAO exists in the outer mitochondrial membrane in liver and brain cells, although some is present in the cytosol in a soluble form. An isolation of a purified soluble monoamine oxidase was achieved from rat liver and brain cells. This preparation was more sensitive to inhibition by the drug deprenyl than by clorgyline and it readily deaminated tyramine and phenylethylamine. Tritiated pargyline bound to the soluble enzyme with less specificity than to the mitochondrial bound enzyme. Polyacrylamide disc gel electrophoresis on soluble MAO produced two broad migrating bands and one stationary band at the origin. In another preparation, one band was found to migrate and the other band remained at the origin. Some properties of the soluble MAO that was isolated are reported in this study.Missing pages 15 and 34.