Glutathione S-transferase of goat lens: evidence for expression of only class mu isoenzymes.
Glutathione S-transferase of goat lens: evidence for expression of only class mu isoenzymes.
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山羊晶状体的谷胱甘肽 S-转移酶：仅表达 mu 类同工酶的证据。
DOI：
10.1076/ceyr.17.11.1097.5230
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发表时间：
1998
影响因子：
2
通讯作者：
Castillo,R
中科院分区：
文献类型：
--
作者：
Ahmad,H;Tobola,AS;Silva,A;Castillo,R
研究表明，哺乳动物眼透镜的谷胱甘肽S-转移酶（GST）可使各种过敏原和白内障原解毒;因此，它可防止白内障的发生。本研究对山羊透镜GST同工酶进行了纯化和鉴定。GST的同工酶通过使用FPLC ®在Mono-P柱上层析聚焦来分离。从山羊透镜中纯化两种GST同工酶GST 7.2和GST 6.6至表观均一性。GST 7.2似乎是Mr.26，500和Mr.25，000亚基的异二聚体，GST 6.6显示Mr.25，000的同源二聚体亚基结构。Western blotting和N端氨基酸序列分析表明，山羊透镜的两种同工酶均属于GST的μ-class。结论山羊透镜的两种同工酶虽然具有不同程度的结构相关性，但可能是两个不同基因的产物。山羊透镜中GST同工酶的表达模式与牛透镜相似，也含有两种GST µ同工酶。
PURPOSEIt has been suggested that glutathione S-transferases (GSTs) of the mammalian ocular lens detoxify various toxi-cants and cataractogens; therefore, it provides protection against cataractogenesis. In this study the GST isoenzymes of goat lens have been purified and characterized.METHODSThe goat lens homogenate was subjected to affinity chromatography over GSH-linked epoxy activated Sepharose 6B. The isoenzymes of the GST were separated by chromato-focusing on a Mono-P column using FPLC ®.RESULTSTwo GST isoenzymes, GST 7.2 and GST 6.6, were purified to apparent homogeneity from goat lens. GST 7.2 appeared to be a heterodimer of Mr. 26,500 and Mr. 25,000 subunits, the GST 6.6 showed a homodimeric subunit structure of Mr. 25,000. Western blotting and the N-terminal region amino acid sequence analysis indicated that both isoenzymes of goat lens belong to the µ-class GST.CONCLUSIONSAlthough they share varying degrees of structural correlation, the two isoenzymes of goat lens seem to be the products of two distinct genes. The isoenzyme expression pat-tern of GST in goat lens is similar to bovine lens, which also contains two isoenzymes belonging only to GST µ.