Walter R D, Ebert F
J Protozool. 1979 Nov;26(4):653-6. doi: 10.1111/j.1550-7408.1979.tb04214.x.
Two glutamate dehydrogenases, NADH-linked (EC 1.2.1.2) and NADPH-linked (EC 1.2.1.4) were isolated from the epimastigote forms of Trypanosoma cruzi and purified. Both enzymes exist as hexamers. The molecular weights of the native NADH-and NADPH-linked glutamate dehydrogenases were estimated to be 360,000 and 265,000, respectively, and those of the subunits to be 58,000 and 43,000, respectively. The isoelectric point of the NADH-linked dehydrogenase is at pH 5.25 and that of the NADPH-linked enzyme at pH 5.1. The activities of both enzymes are regulated by product inhibition. In addition, purine nucleotides were shown to be potent inhibitors of the NADH-linked glutamate dehydrogenase.
从克氏锥虫的无鞭毛体形式中分离并纯化了两种谷氨酸脱氢酶，即NADH连接的（EC 1.2.1.2）和NADPH连接的（EC 1.2.1.4）。这两种酶均以六聚体形式存在。天然NADH连接的和NADPH连接的谷氨酸脱氢酶的分子量分别估计为360,000和265,000，亚基的分子量分别为58,000和43,000。NADH连接的脱氢酶的等电点在pH 5.25，NADPH连接的酶的等电点在pH 5.1。两种酶的活性均受产物抑制调节。此外，嘌呤核苷酸被证明是NADH连接的谷氨酸脱氢酶的有效抑制剂。
