Mixed-mode chromatography (MMC) has been developed as a cost-effective new technique for antibody purification. Nuvia cPrime (NP) is a novel MMC resin with p-aminohippuric acid as the functional ligand. The adsorption of human immunoglobulin G (IgG) and bovine serum albumin (BSA) on NP was measured, including single component adsorption at different pH and binary coadsorption at various pH values and IgG/BSA mass ratios. Typical pH-dependent adsorption behavior was found in the single component adsorption which can be described by a two-parameter equation that offered a convenient way to analyze pH effects. Moreover, a competitive and preferential adsorption of IgG to BSA was investigated in binary coadsorption. Extended Langmuir (EL) and Extended Langmuir-Freundlich (ELF) models with parameters obtained from single-component isotherms were used to describe the coadsorption behaviors of IgG and BSA at various mass ratios. The results indicated the ELF model was more suitable for IgG adsorption, while the EL model was better for describing the weak binding of BSA at pH 7.0 and 8.0.