Abstract
The present study deals with the electrostatic aspects of the interaction between monomeric bovine serum albumin (BSA) and polystyrene latex particles. Adsorption and electrophoresis experiments have been performed as a function of pH, using both negatively and positively charged latices with different surface charge densities. The adsorption isotherms develop well-defined plateaus. These plateaus vary with pH, showing a maximum at the isoelectric point of the protein-covered polystyrene particles, rather than that of the isoelectric point of the protein itself. Co-adsorption of low-molecular-weight ions is shown to be an important parallel process. Studying it helps to discriminate between electrical and chemical contributions to the binding affinity.
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