Purification and properties of monoamineoxidase.
作者： L.M. Barbato , L.G. Abood
DOI: 10.1016/0926-6569(63)90275-X
关键词: Iproniazid 、 Potassium cyanide 、 Oxygen 、 Biochemistry 、 Enzyme 、 Monoamine oxidase 、 Beef Liver 、 Mitochondrion 、 Chemistry 、 Phenanthroline
摘要: Abstract Mitochondrial monoamineoxidase from beef liver has been purified twenty-fold. The enzyme was shown to be metal-dependent by using phenanthroline as an inhibitor. Lineweaver-Burk treatment suggests a non-competitive inhibition. same procedure applied phenylcyclopropylamine shows strictly competitive and irreversible inhibition, the pH-activity curve further presence of two monoamineoxidases. differential action oxygen potassium cyanide on iproniazid inhibition studied, independent cyanide. significance these experiments is discussed.
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