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膜结合大鼠肝脏线粒体单胺氧化酶的反应途径。

The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase.

作者信息

Houslay M D, Tipton K F

出版信息

Biochem J. 1973 Dec;135(4):735-50. doi: 10.1042/bj1350735.

Abstract
  1. A preparation of a partly purified mitochondrial outer-membrane fraction suitable for kinetic investigations of monoamine oxidase is described. 2. An apparatus suitable for varying the O(2) concentration in a spectrophotometer cuvette is described. 3. The reaction catalysed by the membrane-bound enzyme is shown to proceed by a double-displacement (Ping Pong) mechanism, and a formal mechanism is proposed. 4. KCN, NaN(3), benzyl cyanide and 4-cyanophenol are shown to be reversible inhibitors of the enzyme. 5. The non-linear reciprocal plot obtained with impure preparations of benzylamine, which is typical of high substrate inhibition, is shown to be due to aldehyde contamination of the substrate.
摘要
  1. 描述了一种适用于单胺氧化酶动力学研究的部分纯化的线粒体外膜组分的制备方法。2. 描述了一种适用于改变分光光度计比色皿中氧气浓度的装置。3. 膜结合酶催化的反应显示通过双置换(乒乓)机制进行,并提出了一种形式机制。4. 氰化钾、叠氮化钠、苄腈和4-氰基苯酚被证明是该酶的可逆抑制剂。5. 用不纯的苄胺制剂得到的典型高底物抑制的非线性倒数图被证明是由于底物受到醛污染。

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本文引用的文献

1
Tyramine oxidase.酪胺氧化酶
Biochem J. 1937 Oct;31(10):1693-704. doi: 10.1042/bj0311693.
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COMPARATIVE STUDIES IN THE CHARACTERIZATION OF MONOAMINE OXIDASES.单胺氧化酶特性的比较研究
Proc Soc Exp Biol Med. 1963 Dec;114:668-73. doi: 10.3181/00379727-114-28765.

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