Abstract
The preparation and crystallization of l-glutamic dehydrogenase from ox and calf liver is described. The equilibrium constant for the reaction glutamate + = + DPN + + H 2 O ⇌ α- ketoglutarate = + NH 4 + + DPNH − + H + was determined and found to vary somewhat with pH and buffer system. The rate of oxidation of glutamate was also found to vary with pH. Extension of specificity studies resulted in confirmation of the reported strict specificity for l-glutamic acid. No evidence for the nonenzymatic formation of iminoglutaric acid from ammonia and α-ketoglutarate was obtained.
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