Single- and two-solute adsorption breakthrough curves of lysozyme and bovine serum albumin on the cation exchanger SP-Sepharose Fast Flow were studied in this paper. A simplified mathematical model was used to model these data. Input parameters of the model such as equilibrium and kinetic parameters were estimated from single-solute batch experiments. For single-component adsorption in a fixed-bed, the breakthrough behaviour of lysozyme was well modelled. In contrast, significant deviations were observed between the measured and theoretical breakthrough curves of albumin. It was shown that the equilibrium parameters measured from batch experiments failed to account for the behaviour of albumin in the fixed-bed. The bisolute system consisting of the simultaneous adsorption of lysozyme and albumin was also modelled using the same set of parameters derived from single-solute batch experiments. Deviations were observed between the measured and theoretical breakthrough curves for both proteins, indicating that the effects of multicomponent equilibria and kinetics must be taken into consideration in parameter estimation.