Hydrophobic charge-induction chromatography with 4-mercaptoethyl-pyridine as ligands shows promising application in antibody purification. In this study, competitive adsorption of protein mixtures composed with bovine serum albumin (BSA) and immunoglobulin (IgG) was investigated with MEP HyperCel. Static adsorption and dynamic binding processes were measured under different media pH and BSA/IgG mass ratios. The results showed that MEP HyperCel had high pH-dependent selectivity. BSA can be adsorbed quicker than IgG but part of the adsorbed BSA would be gradually displaced by IgG as a result of competitive adsorption. The effects of NaCI and (NH4)(2)SO4 on protein mixture adsorption showed that both salts can enhance IgG selectivity on MEP HyperCel, but the effect was different based on the combination of electrostatic and hydrophobic interactions. Competitive adsorption mechanism was discussed and the results obtained would be useful in the separation of albumin and immunoglobulin from protein mixtures.