人脑中酸性谷胱甘肽S-转移酶6的纯化与鉴定

Purification and characterization of acidic glutathione S-transferase 6 from human brain.

作者信息

Suzuki T, Shaw D C, Board P G

机构信息

Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra.

出版信息

Biochem J. 1991 Mar 1;274 ( Pt 2)(Pt 2):405-8. doi: 10.1042/bj2740405.

DOI:10.1042/bj2740405

PMID:2006908

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1150152/

Abstract

An acidic glutathione S-transferase (GST) isoenzyme termed GST6 has been isolated from human brain, characterized and compared with other isoenzymes. The N-terminal amino acid sequence of GST6 was found to be identical with that of GST4 previously purified from human muscle. GST6 cross-reacted with antibody raised against GST4, but not with antisera raised against GST1, GST2 or GST3. The subunit Mr and pI of GST6 were found to be different from those of GST4. The present results indicate that GST6 is another member of the Mu evolutionary class which in man also includes GST1, GST4 and GST5. A minor component that co-purified with GST6 was shown to have an N-terminal sequence similar to, but not identical with, that of GST3. This isoenzyme may be an additional member of the Pi evolutionary class.

摘要

一种名为GST6的酸性谷胱甘肽S-转移酶（GST）同工酶已从人脑中分离出来，进行了特性鉴定并与其他同工酶进行了比较。发现GST6的N端氨基酸序列与先前从人肌肉中纯化的GST4相同。GST6与针对GST4产生的抗体发生交叉反应，但与针对GST1、GST2或GST3产生的抗血清不发生反应。发现GST6的亚基相对分子质量和等电点与GST4不同。目前的结果表明，GST6是Mu进化类的另一个成员，在人类中该进化类还包括GST1、GST4和GST5。与GST6共纯化的一个次要成分显示其N端序列与GST3相似，但不完全相同。这种同工酶可能是Pi进化类的另一个成员。