Some Properties of the NAD-specific Glutamate Dehydrogenase from Crithidia fasciculata

Summary: The NAD-specific glutamate dehydrogenase from Crithidia fasciculata has been purified 135-fold. Its molecular weight was about 380000. The apparent K m values for 2-oxoglutarate, NADH and NH4Cl were 3, 0.17 and 47 mM, respectively, at pH 7.8, and for l-glutamate and NAD, 10 and 1.4 mM, respectively, at pH 8.6. The enzyme was strongly inhibited by ATP and GTP, and by thiol-binding reagents, such as 5,5'-dithiobis(2-nitrobenzoate) and p-chloromercuribenzoate. Several organic acids, such as pyruvic and l-malic acids, were also inhibitory.

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