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  • Title: [Effect of dissociating agents on Chlorella glutamate dehydrogenases].
    Author: Kasparova MA, Shatilov VR, Kretovich VL.
    Journal: Biokhimiia; 1977 Apr; 42(4):754-6. PubMed ID: 870092.
    Abstract:
    Effect of urea beta-mercaptoethanol and guanidine--hydrochloride on two Chlorella glutamate dehydrogenases (GDH's) have been studied. Both GDH's are inactivated irreversibly by 2-3 M guanidine hydrochloride. Urea above 4 M rapidly inactivates only NH+4-induced NADP--GDH. Constitutive NAD(P)--GDH is stable in 8M urea solution at room temperature for a long time. beta-Mercaptoethanol does not effect significantly the stability of constitutive GDH in 8m urea. Urea above 1M being in reaction mixture inhibits constitutive GDH in a competitive manner to L-glutamate and uncompetitively regards to alpha-oxoglutarate. Taking this into account, one may conclude that L-glutamate and alpha-oxoglutarate seems to bind to different groups on the enzyme molecule.
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