Abstract
Formation of protein-polyelectrolyte complexes (PPCs) between bovine serum albumin (BSA) and potassium poly (vinyl alcohol) sulfate (KPVS) was studied at pH 3 as a function of ionic strength. Turbidimetric titration was employed by a combination of dynamic light scattering (DLS) and electrophoretic light scattering (ELS). The formal charge ( Z PPC) of the resulting PPCs at different ionic strengths were estimated from ELS data by assuming the free draining and the non-free draining model. The radius of a BSA molecule in the complex was used in the former model for calculation of Z PPC with the Henry's equation, while in the latter case the hydrodynamic radius of a PPC particle determined from DLS was employed. The results obtained were compared with the Z PPC values calculated using a relation of Z PPC = n b Z BSA + α Z KPVS , where Z BSA (≥0) and Z KPVS (≤0) denote the formal charge of BSA and KPVS, respectively. Moreover, n b is the number of bound proteins per complex composed of α polymer chains. It was suggested that the PPC between BSA and KPVS behaves as a free draining molecule during the electrophoresis, at least at a high ionic strength. Also suggested is that the PPC formation at low ionic strength follows a 1:1 stoichiometry in the charge neutralization.
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