The adsorption of human IgG onto GMA (a semirigid methacrylate-based chromatography matrix) and His-GMA adsorbents was studied by chromatography and batch equilibrium binding analysis. IgG molecules adsorbed onto GMA gel by nonspecific hydrophobic interactions and the specificities were similar for both adsorbents. Adsorption data were analyzed using three isotherm models, namely the Langmuir, Freundlich and Langmuir-Freundlich models, and the adsorption parameters were computed. The experimental isotherms were best described by a combined Langmuir-Freundlich model, which indicated the presence of unequal binding sites on both adsorbents and/or positive cooperativity in the binding of the IgG molecules.