Scattering correction to the absorbance, wavelength dependence of the refractive index increment, and molecular weight of the bovine liver glutamate dehydrogenase oligomer and subunits

Abstract

Abstract The wavelength dependence of the refractive index increments of bovine serum albumin and bovine liver glutamate dehydrogenase solutions was determined in the range 650–300 nm. It was shown, by measuring the extinction coefficients of glutamate dehydrogenase under conditions of widely differing molecular weights, that a significant scattering correction need not be applied to correct extinction measurements in the absorbtion band. The molecular weight of glutamate dehydrogenase oligomer determined by light scattering and sedimentation equilibrium agrees with the value calculated from the primary structure, if a recently reported value of the extinction coefficient is used.