Hirrell P A, Hume R, Fryer A A, Collins M F, Drew R, Bradwell A R, Strange R C
Department of Postgraduate Medicine, University of Keele, Staffordshire, U.K.
Biochim Biophys Acta. 1987 Oct 15;915(3):371-7. doi: 10.1016/0167-4838(87)90022-7.
The developmental expression of the basic, near-neutral and acidic isoenzymes of glutathione S-transferase (RX:glutathione R-transferase, EC 2.5.1.18) has been studied in heart and diaphragm. Neither these enzymes nor the putative muscle-specific GST4 isoenzyme demonstrated any developmental trends in expression. In vitro hybridisation and SDS-discontinuous polyacrylamide gel electrophoresis were used to show that the GST4 isoenzyme is a homodimer composed of monomers that have a slightly larger molecular weight than the near-neutral isoenzyme. The sensitivity of GST4 to inhibitors also appeared similar to that of the GST1 2 isoenzyme. Immunodiffusion and immunoblotting techniques were used to show that the acidic enzyme in muscle is immunologically identical to that in other tissues.
已对心脏和膈肌中谷胱甘肽S-转移酶(RX:谷胱甘肽R-转移酶,EC 2.5.1.18)的碱性、近中性和酸性同工酶的发育表达进行了研究。这些酶以及假定的肌肉特异性GST4同工酶在表达上均未显示出任何发育趋势。体外杂交和SDS-不连续聚丙烯酰胺凝胶电泳用于表明GST4同工酶是由分子量略大于近中性同工酶的单体组成的同二聚体。GST4对抑制剂的敏感性似乎也与GST1 2同工酶相似。免疫扩散和免疫印迹技术用于表明肌肉中的酸性酶在免疫上与其他组织中的酸性酶相同。