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一种对1-萘基硫酸盐具有活性的人θ类谷胱甘肽S-转移酶的特性分析

Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate.

作者信息

Hussey A J, Hayes J D

机构信息

University Department of Clinical Biochemistry, Royal Infirmary, Edinburgh, Scotland, U.K.

出版信息

Biochem J. 1992 Sep 15;286 ( Pt 3)(Pt 3):929-35. doi: 10.1042/bj2860929.

DOI:10.1042/bj2860929
PMID:1417752
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1132992/
Abstract

A purification scheme is described for a glutathione S-transferase (GST) from human liver that catalyses the conjugation of 1-menaphthyl sulphate (MS) with GSH; the method devised results in an approx. 500-fold increase in specific activity towards MS. The human enzyme which metabolizes MS is a homodimer comprising subunits of M(r) 25,100, and immunochemical experiments have shown it to be a member of the class-Theta GSTs. Automated Edman degradation of this enzyme has confirmed that it is a Theta-class GST bu the amino acid sequence obtained differs from that of GST theta described previously [Meyer, Coles, Pemble, Gilmore, Fraser & Ketterer (1991) Biochem. J. 274, 409-414]. We have therefore designated the enzyme that catalyses the conjugation of MS with GSH GST T2-2* (in the absence of complete amino acid sequence data, the T1 and T2 subunits are provisionally designated T1* and T2*); the evidence which indicates that GST theta (which should possibly now be called GST T1-1*) and GST T2-2* represent distinct isoenzymes is discussed.

摘要

本文描述了一种从人肝脏中纯化谷胱甘肽S-转移酶(GST)的方法,该酶催化1-萘基硫酸盐(MS)与谷胱甘肽(GSH)的结合;所设计的方法使对MS的比活性提高了约500倍。代谢MS的人源酶是一种同型二聚体,由分子量为25,100的亚基组成,免疫化学实验表明它是Theta类GST的成员。对该酶进行自动Edman降解已证实它是Theta类GST,但所获得的氨基酸序列与先前描述的GST theta的序列不同[Meyer, Coles, Pemble, Gilmore, Fraser & Ketterer (1991) Biochem. J. 274, 409 - 414]。因此,我们将催化MS与GSH结合的酶命名为GST T2-2*(在没有完整氨基酸序列数据的情况下,T1和T2亚基暂时命名为T1和T2);文中讨论了表明GST theta(现在可能应称为GST T1-1*)和GST T2-2*代表不同同工酶的证据。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e589/1132992/68d457b7ae2c/biochemj00127-0263-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e589/1132992/68d457b7ae2c/biochemj00127-0263-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e589/1132992/68d457b7ae2c/biochemj00127-0263-a.jpg

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