Nishinaka T, Fujioka M, Nanjo H, Nishikawa J, Mizoguchi T, Terada T, Nishihara T
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Biochem Biophys Res Commun. 1991 May 15;176(3):966-71. doi: 10.1016/0006-291x(91)90376-i.
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-pi and anti-rat glutathione S-transferase-P antibody crossreacted to pig enzyme.
从猪晶状体胞质溶胶中纯化出了Pi类谷胱甘肽S-转移酶,使其达到了均一性。通过SDS凝胶电泳、凝胶过滤、氨基酸序列分析和等电聚焦结果表明,该酶由两个相同的22 kDa亚基组成,等电点为8.5。N端15个残基的氨基酸序列与来自人、大鼠和小鼠的Pi类酶几乎相同。针对猪酶的抗体与人谷胱甘肽S-转移酶-pi发生交叉反应,抗大鼠谷胱甘肽S-转移酶-P抗体与猪酶发生交叉反应。