Effect of pH on the kinetics of bovine liver glutamate dehydrogenase self-association.
The temperature-jump technique with light-scattering detection was applied to the kinetic study on the self-association of bovine liver glutamate dehydrogenase (EC 1.4.1.3). The measurements were carried out for systems in phosphate buffer of differing pH, 6.3-7.8, and of differing phosphate concentration at 11.5 degrees C. The observed association rate constant decreased with increasing phosphate concentration at the respective pH values. This observation was interpreted in terms of the inhibition from self-association by specific binding of phosphate ion to the protein. According to this interpretation, the intrinsic association rate constant, k(0)a, and the binding constant of phosphate ion, Kp, were estimated. k(0)a varied with pH in a manner as described by a titration curve with pK of about 7, while Kp remained almost constant in the pH range studied.
D000818:Animals; D002417:Cattle; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008433:Mathematics; D013696:Temperature
D046911:Macromolecular Substances; D005969:Glutamate Dehydrogenase