Singh S V, Srivastava S K, Awasthi Y C
Exp Eye Res. 1985 Aug;41(2):201-7. doi: 10.1016/0014-4835(85)90025-9.
Human lens has two forms of glutathione S-transferase having pI values of greater than 10 and 4.4. Both of these enzymes may have been purified to an apparent homogeneity from normal human lenses using glutathione affinity chromatography and isoelectric focusing. These two isoenzymes are significantly different from each other in their kinetic, structural, and immunological properties. The cationic form (pI greater than 10) is a dimer of Mr 24 500 subunits whereas the anionic form (pI 4.4) is a dimer of Mr 22 500 subunits. Neither of the two forms express selenium-independent glutathione peroxidase II activity.
人晶状体有两种谷胱甘肽S-转移酶，其等电点分别大于10和4.4。使用谷胱甘肽亲和层析和等电聚焦，这两种酶都可能已从正常人晶状体中纯化至表观均一性。这两种同工酶在动力学、结构和免疫学性质上彼此显著不同。阳离子形式（等电点大于10）是由Mr 24 500亚基组成的二聚体，而阴离子形式（等电点4.4）是由Mr 22 500亚基组成的二聚体。这两种形式均不表达不依赖硒的谷胱甘肽过氧化物酶II活性。
