LIGHT-SCATTERING, ELECTROPHORESIS, AND TURBIDIMETRY STUDIES OF BOVINESERUM-ALBUMIN POLY(DIMETHYLDIALLYLAMMONIUM CHLORIDE) COMPLEX

Complexation between bovine serum albumin (BSA) and poly(dimethyldiall ylammonium chloride) (PDMDAAC) was studied by static and quasi-elastic light scattering (QELS), electrophoretic light scattering, and turbid imetric titration in dilute electrolyte solution. Both QELS and turbid imetric titration show that complexation occurs at pH > 4.6. The struc ture of the BSA-PDMDAAC complex in excess protein solution at ionic st rength 0.01 M and pH 7.88 depends on the polymer concentration. At low polymer concentration, an intrapolymer complex saturated with BSA is formed. This intrapolymer complex aggregates to interpolymer species u pon increase in the polymer concentration.