Preparation and properties of an electrophoretically homogeneous monoamine oxidase from monkey intestine.
作者： D.K. Murali , A.N. Radhakrishnan
DOI: 10.1016/0005-2744(70)90082-3
关键词: Monoamine oxidase 、 Iproniazid 、 Chemistry 、 Sepharose 、 Oxidoreductase 、 Kynuramine 、 Chromatography 、 Polyacrylamide 、 Monoamine neurotransmitter 、 Biochemistry 、 Enzyme
摘要: Abstract The monoamine oxidase (monoamine:O2 oxidoreductase (deaminating), EC 1.4.3.4)) from monkey small intestinal mitochondria has been purified by using (NH4)2SO4 and Sepharose 4B fractionation, the preparation was homogeneous electrophoresis on polyacrylamide gels. enzyme optimally active at pH 7.6 exhibited maximal rates with kynuramine as substrate. moderately inhibited metal chelating agents severely p- hydroxymercuribenzoate . Several inhibitors such Parnate, Iproniazid Niamide showed complete inhibition 0.1 mM, while 1-phenyl-2-isopropylhydrazine (0.1 mM) only 50% inhibition. There no evidence of any multiplicity during fractionation.
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