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[人晶状体中谷胱甘肽-S-转移酶同工酶的研究]

[Investigation of glutathione-S-transferase isozymes in human lenses].

作者信息

Sekine Y, Hommura S, Harada S

机构信息

Eye Clinic, Hitachi General Hospital, Japan.

出版信息

Nippon Ganka Gakkai Zasshi. 1992 Jul;96(7):841-4.

PMID:1502982
Abstract

Glutathione-S-Transferase (GST) isozymes in human lenses were investigated by the immunoenzymatic method using antibody against human liver GST2 and GST3 after polyacrylamide gel isoelectric focusing (western blotting method). Also, rocket immunoelectrophoresis was carried out for the detection of GST1. It was found that GST1 in lens also showed a polymorphism. The GST2 was not found in human clear lenses as well cataractous lenses. In addition, crossreacting materials against both antisera of GST2 and 3 were detected in the pH 6-7 area of the gel in all human lenses.

摘要

采用免疫酶法,利用抗人肝GST2和GST3抗体,在聚丙烯酰胺凝胶等电聚焦后(蛋白质印迹法)对人晶状体中的谷胱甘肽-S-转移酶(GST)同工酶进行了研究。此外,还进行了火箭免疫电泳以检测GST1。结果发现晶状体中的GST1也表现出多态性。在人透明晶状体和白内障晶状体中均未发现GST2。此外,在所有人类晶状体凝胶的pH 6 - 7区域检测到了与GST2和3两种抗血清发生交叉反应的物质。

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