Urea-Induced Inactivation and Dissociation of NAD-Specific Glutamate Dehydrogenase of Neurospora and its Reversal by Substrates

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Abstract
The NAD-specific glutamate dehydrogenase is partially inactivated by 1.5 M and 2.0 M urea. The same concentrations of urea also catalyze a cleavage of the native enzyme into partially active sub-units, approximately half its size. On removal of urea, by passage of the denaturation mixture through a Sephadex G-25 column, the dissociated subunits undergo reassociation restoring the native structure. The presence of substrates NADH and 2-oxoglutarate during renaturation enhances the rate of reassociation and reactivation considerably.

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