作者: Sakari Nara , Benedict Gomes , Kerry T. Yasunobu
DOI: 10.1016/S0021-9258(18)96531-2
关键词: Oxidative enzyme 、 Tyramine 、 Chromatography 、 Biochemistry 、 Enzyme 、 Homogenization (biology) 、 Diethylaminoethyl cellulose 、 Amine oxidase 、 Monoamine oxidase 、 Monoamine oxidase A 、 Chemistry
摘要: Beef liver mitochondrial monoamine oxidase was purified as much 58-fold by a procedure involving disruption of the mitochondria homogenization and Triton X-100 treatment, ammonium sulfate fractionation, alumina gel Cγ chromatography on diethylaminoethyl cellulose. The yielded preparations enzyme which were soluble others still required detergent for solubility in aqueous solutions. substrate specificity, pH optimum, sensitivity to sulfhydryl reagents, other properties indicated that is classical oxidase. From metal analyses enzyme, it demonstrated beef copper-containing protein. purest contained about 0.07% copper. Other metals known be present oxidative enzymes insignificant amounts. copper shown cupric state. Known copper-chelating agents inhibited cuprizone mixed inhibitor enzyme.