The effect of neutral salt anions on the oxidative deamination activity of plant glutamate dehydrogenase.

Increasing concentrations of anions of the Hofmeister series decrease the activity of highly purified glutamate dehydrogenase (EC 1.4.1.2.) from Pisum sativum L. The extent of the inactivation, as estimated by the ion concentration which causes a 50% transformation of the native form to the low activity form of the enzyme (approximately "halfmaximal activity"), follows the ranking Cl(-)<F(-)<Br(-)<NO 3 (-) <SCN(-). Sulfate has a slightly activating effect. At salt concentrations higher than 1 M (with SCN(-) higher than 200 mM), the activity decreases to a value from 3-6% of the initial activity and remains then stable over a wide range of higher anion concentrations. From kinetic investigations it is seen that the treatment of the enzyme with anions decreases the affinity for the cosubstrate NAD(+) and the substrate L-glutamate (K M-values increased) and also increases the dissociation constant for NAD(+). The salt induced inactivation is reversible by dilution. From a mathematical treatment of the kinetic data of the inactivation, it is seen that increasing concentrations of the anions exert cooperative effects on the inactivation process.