Abstract
The effect of various salts on the enzymatic activity of beef‐liver glutamate dehydrogenase, on the binary enzyme‐reduced coenzyme (NADH or NADPH) comples, as well as on the ternary complex with glutamate was investigated in aqueous solution (0.067__M__ phosphate buffer, pH 7.6). Binding studies in the analytical ultracentrifuge and circular dichroism measurements indicated dissociation of the coenzyme from the enzyme‐coenzyme complex by the action of various salts. The efficiency of this change was largely dependent on the type of anion present and generally followed the series: acetate < Br^−^ < I^−^ < SCN^−^. Acetate ions and guanidinium thiocyanate showed exceptional behaviour in some cases, while K^+^ and Na^+^ gave similar results. The reversibility of the ion effects on the enzymatic activity was demonstrated by dilution tests. Upon addition of salts, the inhibitory effect of GTP was slightly changed in most cases, while the activating effects of ADP and L‐leucine were practically abolished and with ADP, the halides caused an additional inhibition. Assuming an equilibrium involving dissociation of the enzyme‐coenzyme complex by the action of salts, an exponent of 1.3 for NaBr and of 2.0 for KSCN was calculated for the respective concentrations. The apparent equilibrium constants were evaluated to be about 20 times greater for KSCN than for NaBr.