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鸡肝脏θ类谷胱甘肽S-转移酶CL1的氨基酸测序、分子克隆及建模

Amino acid sequencing, molecular cloning and modelling of the chick liver class-theta glutathione S-transferase CL1.

作者信息

Hsiao C D, Martsen E O, Lee J Y, Tsai S P, Tam M F

机构信息

Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, R.O.C.

出版信息

Biochem J. 1995 Nov 15;312 ( Pt 1)(Pt 1):91-8. doi: 10.1042/bj3120091.

DOI:10.1042/bj3120091
PMID:7492340
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1136231/
Abstract

Glutathione S-transferase CL1-2 heterodimers purified from 1-day-old chick livers were digested with Achromobacter proteinase I. The resulting fragments were separated for amino acid sequence analysis. Oligonucleotide probes were constructed based on sequence similarity to class-Theta glutathione S-transferases for PCR using a chicken liver cDNA library as template. A full-length clone (1725 bp) encoding a polypeptide comprising 261 amino acids was isolated. Including conservative substitutions, this protein has 70-73% sequence similarity with other mammalian class-Theta glutathione S-transferases. Based on known X-ray crystal structures of class-Alpha, -Mu and -Pi glutathione S-transferases, a model is constructed for the N-terminal 232 residues of CL1.

摘要

从1日龄雏鸡肝脏中纯化的谷胱甘肽S-转移酶CL1-2异二聚体用嗜麦芽窄食单胞菌蛋白酶I进行消化。将所得片段分离以进行氨基酸序列分析。基于与Theta类谷胱甘肽S-转移酶的序列相似性构建寡核苷酸探针，以鸡肝cDNA文库为模板进行PCR。分离出一个编码包含261个氨基酸的多肽的全长克隆（1725 bp）。包括保守性替换在内，该蛋白与其他哺乳动物Theta类谷胱甘肽S-转移酶具有70-73%的序列相似性。基于已知的Alpha类、Mu类和Pi类谷胱甘肽S-转移酶的X射线晶体结构，构建了CL1 N端232个残基的模型。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1cf5/1136231/4665d8ddd467/biochemj00051-0100-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1cf5/1136231/4665d8ddd467/biochemj00051-0100-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1cf5/1136231/4665d8ddd467/biochemj00051-0100-a.jpg

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本文引用的文献

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