Optimal Conditions for the Kinetic Assay of Serum Glutamate Dehydrogenase Activity at 37°C

Abstract

Abstract Optimal concentrations of ammonium ions, 2-oxoglutarate, and NADH were defined for serum glutamate dehydrogenase (EC 1.4.1.2) activity at 37°C. Substrate inhibition was not observed with the last two compounds. The pH optimum in triethanolamine buffer is 7.4, and activity is inhibited by increasing the buffer concentration beyond 50 mmol/liter. Activation by ADP exceeds that promoted by L-leucine, and there is little advantage in having both present. Activity is linear with time and with enzyme concentration to a limiting absorbance change of 0.300 at 340 nm, and precision was satisfactory. Data indicate the normal range to lie between 0 and 4 U/liter.