Majerus P W, Brauner M J, Smith M B, Minnich V
J Clin Invest. 1971 Aug;50(8):1637-43. doi: 10.1172/JCI106652.
The two enzymes required to synthesize glutathione de novo have been purified from human erythrocytes. Glutamylcysteine synthetase was purified 4300-fold and was approximately 80% pure based on polyacrylamide gel electrophoresis. The purified enzyme catalyzes the formation of 30.5 mumoles of gamma-glutamyl-cysteine per mg of protein per hr and is inhibited by sulfhydryl inhibitors. Glutathione synthetase was purified 6000-fold from erythrocytes to homogeneity as determined by polyacrylamide gel electrophoresis. The erythrocyte enzyme has a molecular weight of 150,000 and catalyzes the formation of 35.9 mumoles of glutathione per mg of protein per hr. Comparison of the amino acid composition and some kinetic parameters of yeast glutathione synthetase and the erythrocyte enzyme demonstrate similarities between these enzymes.
从头合成谷胱甘肽所需的两种酶已从人红细胞中纯化出来。谷氨酰半胱氨酸合成酶被纯化了4300倍，根据聚丙烯酰胺凝胶电泳，其纯度约为80%。纯化后的酶每毫克蛋白质每小时催化形成30.5微摩尔的γ-谷氨酰半胱氨酸，并受到巯基抑制剂的抑制。谷胱甘肽合成酶从红细胞中纯化了6000倍，达到聚丙烯酰胺凝胶电泳所确定的均一性。红细胞酶的分子量为150,000，每毫克蛋白质每小时催化形成35.9微摩尔的谷胱甘肽。对酵母谷胱甘肽合成酶和红细胞酶的氨基酸组成及一些动力学参数进行比较，结果表明这些酶之间存在相似性。
