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Quasielastic light scattering spectroscopy was used to study the mutual diffusion coefficient Dm of bovine serum albumin over the pH range 4.3–7.6 for concentrations ranging as high as 334 g/l. Using literature measurements of the tracer diffusion coefficient DT and the osmotic compressibility (∂π/∂c)P,T, we find that Dm depends on concentration and pH as predicted by the generalized Stokes–Einstein relation Dm=DT(∂π/∂c)P,T (1−φ)/KBT, φ being the volume fraction of solute and KB being Boltzmann’s constant. Our data show that Dm and DT depend quite differently on solute concentration; DT can be a factor of 3 smaller than Dm at protein concentrations exceeding 200 g/l.
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Phillies et al. (1976) studied this question.
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