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 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 -chloromercuribenzoate. Several organic acids, such as pyruvic and l-malic acids, were also inhibitory.

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/content/journal/micro/10.1099/00221287-113-2-429
1979-08-01
2019-10-16
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-113-2-429
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