Interaction between serum albumin and water at different concentrations of hydrogen ions based on data from Rayleigh scattering

Diluted solutions of serum albumin in water are studied at different values of the total surface charge in protein using a Rayleigh light scattering method. It is shown that the effective electron polarizability, the second virial coefficient, the degree of depolarization, and the parameters of the tensor of polarizability of the macromolecules of the protein are a nonlinear function of the pH of the solution and have an extremum at the isoelectric point.