Satoh K, Hatayama I, Tsuchida S, Sato K
Second Department of Biochemistry, Hirosaki University, School of Medicine, Japan.
Arch Biochem Biophys. 1991 Mar;285(2):312-6. doi: 10.1016/0003-9861(91)90365-p.
Investigation of biochemical characteristics of the glutathione S-transferase P-form (GST 7-7), a specific marker enzyme for preneoplastic cells arising during chemical hepatocarcinogenesis in the rat, revealed distinct functional differential from six other major GST forms. While the GST 7-7 substrate specificity was generally broader, binding ability for diverse organic anions such as bilirubin, hematin, and sulfobromophthalein was as high as in any of the other six forms. Furthermore, the enzymatic activity of GST 7-7 was found to be highly insensitive to the inhibitory actions of a wide range of organic anions at physiological pH in contrast to the other forms which proved more susceptible. The functional characteristics of GST 7-7 may in part account for its overproduction in the preneoplastic cells.
对谷胱甘肽S-转移酶P型(GST 7-7)生化特性的研究表明,它是大鼠化学性肝癌发生过程中癌前细胞的一种特异性标记酶,与其他六种主要的GST形式存在明显的功能差异。虽然GST 7-7的底物特异性通常更广,但它对胆红素、血红素和磺溴酞钠等多种有机阴离子的结合能力与其他六种形式中的任何一种一样高。此外,与其他更易受影响的形式相比,发现GST 7-7的酶活性在生理pH值下对多种有机阴离子的抑制作用高度不敏感。GST 7-7的功能特性可能部分解释了它在癌前细胞中的过量产生。