Hayes J D, Chalmers J
Biochem J. 1983 Dec 1;215(3):581-8. doi: 10.1042/bj2150581.
A purification scheme is described for the neutral glutathione S-transferases of rat liver. Discontinuous sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that one of these enzymes contains a previously unidentified subunit, which has a molecular mass of 23 000 Da and has been designated Yn. Bile acids inhibited the activity of all the basic and neutral transferases investigated, but marked differences in the effects of bile acids on individual enzymes were observed. The activity of each transferase was inhibited more by lithocholate 3-sulphate than by chenodeoxycholate, which in turn was more inhibitory than cholate. The enzymes that were most sensitive to cholate inhibition were not found to be as readily inhibited as other transferases by chenodeoxycholate or lithocholate 3-sulphate. Conversely, the activity of transferase AA was more resistant to cholate, chenodeoxycholate and lithocholate 3-sulphate inhibition than was any of the other enzymes studied.
本文描述了一种用于大鼠肝脏中性谷胱甘肽S-转移酶的纯化方案。不连续十二烷基硫酸钠/聚丙烯酰胺凝胶电泳显示，其中一种酶含有一个先前未鉴定的亚基，其分子量为23000道尔顿，被命名为Yn。胆汁酸抑制了所有研究的碱性和中性转移酶的活性，但观察到胆汁酸对各酶的影响存在显著差异。与鹅去氧胆酸相比，3-硫酸石胆酸对每种转移酶活性的抑制作用更强，而鹅去氧胆酸的抑制作用又强于胆酸。未发现对胆酸抑制最敏感的酶像其他转移酶那样容易被鹅去氧胆酸或3-硫酸石胆酸抑制。相反，转移酶AA的活性比所研究的任何其他酶对胆酸、鹅去氧胆酸和3-硫酸石胆酸的抑制作用更具抗性。
