Organization of Krebs tricarboxylic acid cycle enzymes

Jack B. Robinson Jr. , Paul A. Srere
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引用次数: 13

Abstract

Binding of enzymes of the Krebs TCA cycle to biological membranes was characterized with respect to intracellular location, susceptibility to various chemical and physical treatments, and extractability as a macromolecular component of the mitochondrial inner membrane. It was shown that citrate synthase and malate dehydrogenase bind to the inner membrane in an ionic strength-sensitive, saturable, and specific manner to a relatively thermostabile component manifested on the inner (matrix) surface of the inner membrane of the mitochondrion. From these data several arguments in support of the physiological applicability of these processes were educed, and the question of whether these two enzymes bind to the same or different membrane components was considered. Also, experiments preliminary to purification of the citrate synthase binding component were presented.

克雷布斯三羧酸循环酶的组织
Krebs TCA循环的酶与生物膜的结合在细胞内的位置、对各种化学和物理处理的敏感性以及作为线粒体内膜的大分子成分的可提取性方面进行了表征。结果表明,柠檬酸合成酶和苹果酸脱氢酶以离子强度敏感、饱和和特异性的方式与线粒体内膜内(基质)表面的相对热稳定性组分结合。从这些数据中得出了支持这些过程的生理适用性的几个论点,并考虑了这两种酶是否与相同或不同的膜组分结合的问题。并对柠檬酸合酶结合组分的纯化进行了初步实验。
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