McLellan L I, Wolf C R, Hayes J D
University Department of Clinical Chemistry, Royal Infirmary, Edinburgh, Scotland, U.K.
Biochem J. 1989 Feb 15;258(1):87-93. doi: 10.1042/bj2580087.
A microsomal glutathione S-transferase (GST) was purified from human liver. This enzyme was shown to have characteristics similar to those of the rat microsomal GST described by Morgenstern & De Pierre [(1983) Eur. J. Biochem. 134, 591-597]. The specific activity of human microsomal GST towards 1-chloro-2,4-dinitrobenzene or cumene hydroperoxide can be stimulated by treating the enzyme with N-ethylmaleimide. This enhancement of activity is accompanied by increased sensitivity to inhibition by haematin and cholic acid. The subunit Mr values of the rat and human enzymes are similar (approx. 17,300), and the proteins are immunologically related. During purification, both human and rat microsomal GST enzymes are the only hepatic proteins obtained from Triton X-100-solubilized microsomal fractions that show activity towards the nephrotoxin hexachlorobuta-1,3-diene. The involvement of microsomal GST in toxification reactions is discussed.
从人肝脏中纯化出一种微粒体谷胱甘肽S-转移酶(GST)。已证明该酶具有与Morgenstern和De Pierre所描述的大鼠微粒体GST相似的特性[(1983年)《欧洲生物化学杂志》134卷,591 - 597页]。用人微粒体GST对1-氯-2,4-二硝基苯或氢过氧化异丙苯的比活性可通过用N-乙基马来酰亚胺处理该酶来刺激。活性的这种增强伴随着对血红素和胆酸抑制的敏感性增加。大鼠和人酶的亚基相对分子质量值相似(约17,300),并且这两种蛋白质在免疫学上相关。在纯化过程中,人和大鼠微粒体GST酶是从Triton X-100增溶的微粒体组分中获得的仅有的对肾毒素六氯丁二烯1,3-二烯有活性的肝脏蛋白质。讨论了微粒体GST在解毒反应中的作用。