Board P G, Pierce K
Department of Human Genetics, John Curtin School of Medical Research, Australian National University, Canberra.
Biochem J. 1987 Dec 15;248(3):937-41. doi: 10.1042/bj2480937.
A plasmid, termed pTacGST2, which contains the complete coding sequence of a GST2 (glutathione S-transferase 2) subunit and permits the expression of the protein in Escherichia coli was constructed. The expressed protein had the same subunit Mr as the enzyme from normal human liver and retained its catalytic function with both GST and glutathione peroxidase activity. Antiserum raised against the bacterially synthesized protein cross-reacted with all the basic GST isoenzymes in human liver. The electrophoretic mobility in agarose of the bacterially expressed isoenzyme suggested that its pI is identical with that of the cationic isoenzyme from human liver previously termed GST2 type 1. The available evidence suggests that the three common cationic isoenzymes found in human liver are the products of two very similar gene loci.
构建了一种名为pTacGST2的质粒，它包含谷胱甘肽S-转移酶2（GST2）亚基的完整编码序列，并能使该蛋白在大肠杆菌中表达。所表达的蛋白与正常人肝脏中的酶具有相同的亚基分子量，并保留了其谷胱甘肽S-转移酶和谷胱甘肽过氧化物酶活性的催化功能。针对细菌合成蛋白产生的抗血清与人肝脏中的所有碱性谷胱甘肽S-转移酶同工酶发生交叉反应。细菌表达的同工酶在琼脂糖中的电泳迁移率表明其pI与先前称为GST2 1型的人肝脏阳离子同工酶相同。现有证据表明，在人肝脏中发现的三种常见阳离子同工酶是两个非常相似基因座的产物。
