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Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion
Author(s) -
Minton Allen P.,
Edelhoch H.
Publication year - 1982
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360210215
Subject(s) - chemistry , bovine serum albumin , scattering , electrostatics , light scattering , particle (ecology) , radius , molecule , electrophoresis , chemical physics , analytical chemistry (journal) , crystallography , chromatography , optics , physics , organic chemistry , oceanography , computer security , computer science , geology
The light scattering of bovine serum albumin (BSA) has been measured at protein concentration up to 90 g/L and at pH values between 4.4 and 7.6. The dependence of scattering on both protein concentration and pH may be quantitatively accounted for by a simple extension of the hard‐sphere model for protein solutions [Ross, P. D. & Minton, A. P. (1977) J. Mol. Biol. 112 , 437–452] allowing for electrostatic repulsions between molecules. According to the extended model, the radius of the effective hard spherical particle representing BSA varies with the net electrical charge of the BSA molecule in a manner which may be calculated from electrostatic theory.