Angular dependence of scattered light, rotary frictional coefficients, and distribution of sizes of associated oligomers in solutions of bovine liver glutamate dehydrogenase.

Abstract

AbstractThe angular dependence of scattering in solutions of bovine liver glutamate dehydrogenase was studied in 0.2M Na‐phosphate buffer, pH 7, 10−4M EDTA, and in buffered solutions saturated with either toluene or benzene. Whereas the shape of the scattering curves is in qualitative accord with the previously reported polymerization to rodlike linear structures, quantitative agreement between the calculated and experimental curves is poor when the polydispersity consistent with the association mechanism (derived from molecular weight determinations by light scattering and equilibrium sedimentation) is properly taken into account. The measurement of rotary frictional coefficients of macroscopic models of linearly associated glutamate dehydrogenase oligomers allowed the calculation of intrinsic viscosities of enzyme solutions but did not permit discrimination, by hydrodynamic means, between systems with different distributions of length.