Bach M K, Brashler J R
Prostaglandins Leukot Med. 1985 Jan;17(1):125-36. doi: 10.1016/0262-1746(85)90041-1.
The cytosolic glutathione S-transferases of rat liver have been partially purified by affinity adsorption to glutathionyl Sepharose and elution with glutathione, and have been fractionated by chromatofocusing. The column eluates were pooled into ten fractions, although evaluation of the enzymatic activities of the column eluates with different chromogenic substrates indicated that some of the fractions were heterogeneous. The pooled fractions were characterized with respect to their substrate specificity, their susceptibility to inhibition by several inhibitors, and their ability to catalyze the conjugation of glutathione to leukotriene A4. It was found that all the fractions were able to catalyze leukotriene C formation. The fraction having the highest specific activity with three different chromogenic substrates also had the highest specific activity when LTA was used as the substrate while, in general, there were marked differences in the relative activities of the different pooled fractions. The most active fraction represented approximately 50% of the total glutathione S-transferase activity in the whole preparation and had an apparent isoelectric point of 9.05. There was no apparent relationship between the ability of the different fractions to utilize LTA and any of the other substrates which were tested.
大鼠肝脏的胞质谷胱甘肽S - 转移酶已通过亲和吸附到谷胱甘肽琼脂糖上并用谷胱甘肽洗脱进行了部分纯化，随后通过色谱聚焦进行了分级分离。柱洗脱液被合并为十个级分，尽管用不同显色底物对柱洗脱液的酶活性进行评估表明一些级分是异质的。对合并的级分进行了底物特异性、对几种抑制剂抑制作用的敏感性以及催化谷胱甘肽与白三烯A4结合能力的表征。发现所有级分都能够催化白三烯C的形成。在使用三种不同显色底物时具有最高比活性的级分，在以LTA作为底物时也具有最高比活性，而一般来说，不同合并级分的相对活性存在显著差异。活性最高的级分约占整个制剂中总谷胱甘肽S - 转移酶活性的50%，其表观等电点为9.05。不同级分利用LTA的能力与所测试的任何其他底物之间没有明显关系。
