“…Since the scattering power of globular proteins is weak, static and dynamic light scattering experiments can be carried out to relatively high concentrations without problems from multiple scattering artifacts, as confirmed directly by experiment (5). As a framework for the discussion of the effects of ionic strength and pH on the diffusion coefficient of BSA, we utilize the theoretical calculations of Batchelor (13), Felderhoff (15), and Phillies (18), which assume an impermeable hard-sphere model. We compare data on D m and d/dc at the isoelectric pH ϭ 4.7 and I ϭ 0.1, where BSA has a net charge of zero (19), with results at pH ϭ 7.4 and I ϭ 0.15, pH ϭ 7.4 and I ϭ 1.5, and pH ϭ 7.4 and I ϭ 3.3.…”