细胞质硫醇转移酶在通过硫醇-二硫化物交换进行细胞调节中的作用。
Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange.
作者信息
Mannervik B, Axelsson K
出版信息
Biochem J. 1980 Jul 15;190(1):125-30. doi: 10.1042/bj1900125.
Abstract
Cytoplasmic thioltransferase purified from rat liver [Axelsson, Eriksson & Mannervik (1978) Biochemistry 17, 2978--2984] catalyses the formation and decomposition of mixed disulphides of proteins and glutathione. The enzyme was found to catalyse the reversible thiol-disulphide interchange between glutathione disulphide and a crude thiol-containing protein fraction from rat liver. This finding indicates a role of the thioltransferase in the regulation of the 'glutathione status' of the cell. Specifically, it was found that thioltransferase catalyses the reactivation of pyruvate kinase from rat liver that had previously been inactivated by glutathione disulphide. It is suggested that thioltransferase may have a general role in regulatory processes involving thiol-disulphide interchange.
摘要
从大鼠肝脏中纯化得到的细胞质硫醇转移酶[阿克塞尔松、埃里克松和曼内维克（1978年），《生物化学》17卷，2978 - 2984页]催化蛋白质与谷胱甘肽混合二硫键的形成与分解。研究发现该酶能催化谷胱甘肽二硫化物与大鼠肝脏中一种含硫醇的粗蛋白组分之间的可逆硫醇 - 二硫键交换。这一发现表明硫醇转移酶在细胞“谷胱甘肽状态”的调节中发挥作用。具体而言，发现硫醇转移酶能催化先前被谷胱甘肽二硫化物灭活的大鼠肝脏丙酮酸激酶的再活化。有人提出硫醇转移酶可能在涉及硫醇 - 二硫键交换的调节过程中具有普遍作用。
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