Caldas R A, Araújo E F, Felix C R, Roitman I
J Parasitol. 1980 Apr;66(2):213-6.
Ammonium ions were incorporated into L-glutamate and alpha-ketoglutarate in epimastigote forms of Trypanosoma cruzi through the following enzymatic systems: NADPH and NADH-dependent glutamate dehydrogenase, NADPH-dependent glutamate synthase, L-glutamine synthetase and NADH-dependent glutamate synthase in order of decreasing specific activity (mumoles of product formed/min/mg protein). The pH optima and Km's for the glutamate dehydrogenase system were determined. Disc electrophoresis showed the presence of cathodic bands of GDH activity, which were highly dependent on NADP+.
通过以下酶系统，铵离子被掺入克氏锥虫的无鞭毛体形式的L-谷氨酸和α-酮戊二酸中：NADPH和NADH依赖性谷氨酸脱氢酶、NADPH依赖性谷氨酸合酶、L-谷氨酰胺合成酶和NADH依赖性谷氨酸合酶，其比活性（每分钟形成的产物微摩尔数/毫克蛋白质）依次降低。测定了谷氨酸脱氢酶系统的最适pH值和Km值。圆盘电泳显示存在GDH活性的阴极带，其高度依赖于NADP+。
