[A new method of preparing and some properties of high molecular weight monoamine oxidase from swine liver mitochondria].

E B Nikol'skaia, O V Iagodina, B A Grinberg, M M Dianova
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Abstract

Isolation of highly purified and highly molecular monoamine oxidase (MAO) from pig liver mitochondria have been worked out. Specific activity of isolated preparation is 2700 times higher than of original mitochondria homogenate. Enzyme solubilization by digitonin, affinity chromatography purification and ultrafiltration underlie this method. MAO catalytic properties changing during the process of purification by different methods have been investigated. Substrate specificity was studied; kinetic parameters of enzymatic desemination were calculated.

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[从猪肝线粒体制备高分子量单胺氧化酶的新方法及一些性能]。
比活性是原线粒体匀浆的2700倍。该方法的基础是洋地黄苷酶增溶、亲和层析纯化和超滤。研究底物特异性;计算了酶解精的动力学参数。
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