| Abstract: | Measurements of light scattering at 546 nm were carried out on bovine serum albumin in LiCl solutions at neutral pH (ca. 5.2) and room temperature. The concentration of LiCl varied from 0.1 to 7.0 M. There was a relatively small increase in the molecular weight of the protein when the concentration of LiCl in aqueous solutions was in the range between 0.1 M and 3.0 M. A major increase occurred when the concentration of LiCl exceeded 3.0 M. Preferential binding of LiCl to the protein varied in the same direction: negative when the concentration of LiCl was below 3.0 M and positive when the concentration was above 3.0 M. A reaction pattern suggested that the aggregation is preceded by a reversible conformational change of the monomer and the aggregation is a combination of denatured monomers. |
