PIG LENS GLUTATHIONE-S-TRANSFERASE BELONGS TO CLASS-PI ENZYME

被引：14

作者：

NISHINAKA, T ^{[1
]}

FUJIOKA, M ^{[1
]}

NANJO, H ^{[1
]}

NISHIKAWA, JI ^{[1
]}

MIZOGUCHI, T ^{[1
]}

TERADA, T ^{[1
]}

NISHIHARA, T ^{[1
]}

机构：

[1] OSAKA UNIV, FAC PHARMACEUT SCI, BIOCHEM LAB, 1-6 YAMADA OKA, SUITA, OSAKA 565, JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)90376-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Class Pi glutathione S-transferase was purified to homogeneity from pig lens cytosol. This enzyme was composed of two identical 22 kDa subunits and had isoelectric point of 8.5 from the results of SDS gel electrophoresis, gel filtration, amino acid sequence analysis and isoelectric focusing. Amino acid sequence of N-terminal 15 residues was almost identical to class Pi enzymes from human, rat and mouse. Antibody against the pig enzyme crossreacted to human glutathione S-transferase-π and anti-rat glutathione S-transferase-P antibody crossreacted to pig enzyme. © 1991.

引用

页码：966 / 971

页数：6

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