1887

Abstract

Summary: The NAD-specific glutamate dehydrogenase from has been purified 135-fold. Its molecular weight was about 380000. The apparent values for 2-oxoglutarate, NADH and NHCl were 3, 0·17 and 47 m, respectively, at pH 7·8, and for l-glutamate and NAD, 10 and 1·4 m, 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 -chloromercuribenzoate. Several organic acids, such as pyruvic and -malic acids, were also inhibitory.

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/content/journal/micro/10.1099/00221287-113-2-429
1979-08-01
2021-05-15
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