Abstract
Electrostatic aspects of the interaction between monoclonal mouse anti-human chorionic gonadotropin immuno gamma globulins and polystyrene latex particles are reported. Adsorption and electrophoresis experiments have been performed as a function of pH, using both negatively and positively charged latices and monoclonal immuno gamma globulins having different isoelectric points. Adsorption isotherms show high affinity character with well-defined plateaus. The plateaus vary with pH, showing a maximum at the isoelectric point of the protein-covered polystyrene particles, rather than at the isoelectric point of the immuno gamma globulin in solution. Since a similar behaviour has been previously reported for bovine serum albumin this observation might be a more general feature in protein adsorption.
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