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• W1985574773 abstract "We report static and dynamic light scattering measurements on bovine serum albumin (BSA) solutions at high ionic strength (I) where potential and hydrodynamic interactions between BSA molecules are of comparable strengths. Measurements of the concentration dependence of the osmotic compressibility, (dπ/dc), and the translational diffusion coefficient, Dm, are presented for several solvent systems: (a) at the isoelectric pH = 4.7 and I = 0.1, where long-range electrostatic repulsions are absent; (b) at pH = 7.4 and I = 0.15, 1.5, and 3.3, where a well-screened electrostatic repulsion is present. The results are compared with theoretical predictions which involve a microscopic hard-sphere treatment of the potential and hydrodynamic interactions. At pH = 7.4 and I = 1.5, our experimental results for dπ/dc are in good agreement with the hard-sphere prediction, and our values for Dm are, likewise, consistent with a hard-sphere hydrodynamic analysis in which contributions from the divergence terms in the velocity field are neglected. At the isoelectric pH, similar agreement with theory is obtained, provided the contribution of an attractive potential is included; at pH 7.4 and I = 0.15, the contribution from a long-range repulsion must be included; at pH 7.4 and I = 3.3, onset of protein aggregation is observed." @default.
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• W1985574773 date "1999-10-01" @default.
• W1985574773 modified "2023-09-23" @default.
• W1985574773 title "Translational Diffusion Coefficients of Bovine Serum Albumin in Aqueous Solution at High Ionic Strength" @default.
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• W1985574773 doi "https://doi.org/10.1006/jcis.1999.6401" @default.
• W1985574773 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10489290" @default.
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