[Effect of dissociating agents on Chlorella glutamate dehydrogenases].
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.
D002708:Chlorella / Q000201:enzymology*; D004305:Dose-Response Relationship, Drug; D004355:Drug Stability; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors*; D006146:Guanidines / Q000494:pharmacology*; D008623:Mercaptoethanol / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014508:Urea / Q000494:pharmacology*
D006146:Guanidines; D008623:Mercaptoethanol; D014508:Urea; D005969:Glutamate Dehydrogenase
Vliianie dissotsiiruiushchikh agentov na glutamatdegidrogenazy khlorelly