大鼠肝细胞溶胶中硫醇转移酶催化的蛋白质混合二硫键中二硫键的还原。
Reduction of disulphide bonds in proteins mixed disulphides catalysed by a thioltransferase in rat liver cytosol.
作者信息
Mannervik B, Axelsson K
出版信息
Biochem J. 1975 Sep;149(3):785-8. doi: 10.1042/bj1490785.
Abstract
The reduction of mixed disulphides of some proteins and GSH [Protein(-SSG)n] is accomplished with GSH as a reductant and a thioltransferase from rat liver as a catalyst, thus: See article. The spontaneous reaction is negligible in comparison with the enzymic reaction in vivo, and any direct reduction with glutathione reductase is not detectable with the substrates used. The reduction is only indirectly dependent on NADPH, which is required for the regeneration of GSH from GSSG. Other protein disulphides apparently are reduced via analogous GSH-dependent reactions
摘要
某些蛋白质与谷胱甘肽的混合二硫化物[蛋白质(-SSG)n]的还原反应，是以谷胱甘肽作为还原剂、大鼠肝脏中的硫醇转移酶作为催化剂来完成的，具体如下：见文章。与体内的酶促反应相比，自发反应可忽略不计，并且在所使用的底物中，无法检测到谷胱甘肽还原酶的任何直接还原作用。该还原反应仅间接依赖于NADPH，NADPH是将GSSG再生为GSH所必需的。其他蛋白质二硫化物显然也是通过类似的谷胱甘肽依赖性反应被还原的
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