Goldmann D R, Segal S
Enzyme. 1977;22(5):301-11. doi: 10.1159/000458809.
gamma-Glutamyltranspeptidase, known to be localized in the proximal tubule cell brush border in the rat, is a membrane-bound enzyme which transfers the gamma-glutamyl moiety of glutathione or its analogue gamma-glutamyl-p-nitroanilide to an amino acid or dipeptide acceptor. Brush borders were isolated from the kidneys of newborn and adult Sprague-Dawley rats and assayed for gamma-glutamyltranspeptidase activity. There is an increase in specific activity in the brush border with maturation. Newborn and adult brush border preparations exhibit similar pH optima, substrate affinities, apparent Km values, patterns of heat inactivation, inhibition by glutathione, and migration on polyacrylamide gels. Polyacrylamide gel electrophoresis of a deoxycholate extract of brush border proteins and subsequent reaction with substrate within the gel reveal the presence of two bands, suggesting the presence of two forms of gamma-glutamyltranspeptidase in the rat kidney brush border.
γ-谷氨酰转肽酶,已知定位于大鼠近端小管细胞刷状缘,是一种膜结合酶,它将谷胱甘肽或其类似物γ-谷氨酰-对硝基苯胺的γ-谷氨酰部分转移到氨基酸或二肽受体上。从新生和成年Sprague-Dawley大鼠的肾脏中分离出刷状缘,并测定γ-谷氨酰转肽酶活性。随着成熟,刷状缘中的比活性增加。新生和成年刷状缘制剂表现出相似的最适pH值、底物亲和力、表观Km值、热失活模式、谷胱甘肽抑制作用以及在聚丙烯酰胺凝胶上的迁移情况。对刷状缘蛋白的脱氧胆酸盐提取物进行聚丙烯酰胺凝胶电泳,并随后在凝胶内与底物反应,显示有两条带,表明大鼠肾脏刷状缘中存在两种形式的γ-谷氨酰转肽酶。