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The mutual diffusion coefficient Dm was measured by means of photon correlation spectroscopy (PCS) for bovine serum albumin (BSA) at pH 4.7 and ionic strength I≃0.12 M. The BSA concentrations ranged from 1.00 to 10.7 g/dℓ and the magnitude of the scattering wave vector K varied from 3.21×104 to 3.51×105 cm−1. It was found that Dm=D0[1−(0.0166±0.0009)C], where D0=(5.92±0.04)×10−7 cm2/s corrected to water at 20 °C and the C measured in units of g/dℓ. The quantity Cn/K3, where Cn is the concentration in number of solute particles per cm3, ranged from 2 to 27 000, but this had no influence on the measured values of Dm. This work does not support the idea that the small size of K−1 or the small number of molecules contained in the volume K−3 affects the magnitudes of diffusion coefficients determined by PCS for proteins at moderate ionic strengths.
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Oh et al. (1981) studied this question.
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