PROPERTIES AND PHYSIOLOGICAL SIGNIFICANCE OF MULTIPLE FORMS OF MITOCHONDRIAL MONOAMINE OXIDASE (MAO)

摘要: ABSTRACT. Much indirect evidence has accumulated to suggest that monoamine oxidase (MAO) may not be a single enzyme but number of closely related catalysts with different substrate and inhibitor specificities. The is associated the outer membrane mitochondria. Solubilized purified MAO contains one mole covalently bound FAD eight moles -SH per 120,000 g protein. Electrophoresis soluble on polyacrylamide gel exhibits active cathodic anodic bands as visualized by histochemical procedures. properties extracted have revealed they are regard molecular weight, content, subunits binding sites for phenelzine. However exhibit specificities, thermal inactivation, pH optima. multiplicity universally accepted. Because multiple forms contain varying amounts phospholipid material it been suggested represent artifacts purification procedure. strong presented immunologically distinct populations mitochondria in liver brain. physiological role remains elucidated. Drugs irreversibly inhibit this used chemotherapy depressive illness. It therefore these drugs owe their beneficial effect inhibition particular form at specific site brain, thereby raising level transmitter amines.