Abstract
All the glutamate dehydrogenase activity in developing castor bean endosperm is shown to be located in the mitochondria. The enzyme can not be detected in the plastids, and this is probably not due to the inactivation of an unstable enzyme, since a stable enzyme can be isolated from castor bean leaf chloroplasts. The endosperm mitochondrial glutamate dehydrogenase consists of a series of differently charged forms which stain on polyacrylamide gel electrophoresis with both NAD(+) and NADP(+). The chloroplast and root enzymes differ from the endosperm enzyme on polyacrylamide gel electrophoresis. The amination reaction of all the enzymes is affected by high salt concentrations. For the endosperm enzyme, the ratio of activity with NADH to that with NADPH is 6.3 at 250 millimolar NH(4)Cl and 1.5 at 12.5 millimolar NH(4)Cl. K(m) values for NH(4) (+) and NAD(P)H are reduced at low salt concentrations. The low K(m) values for the nucleotides may favor a role for glutamate dehydrogenase in ammonia assimilation in some situations.
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