The simulation of the behaviour of two proteins (cytochrom c and alpha-chymotrypsinogen) on two types of stationary phases (monolithic and porous particle-based) was attempted for non-linear (simulation of breakthrough curves) and linear (simulation of elution peaks) cation exchange chromatography. It was found that the combination of a stoichiometric model (steric mass action, SMA) with the lumped pore diffusion (POR) model allows a simulation of high predictive value. Using one set of SMA and transport parameters for a given column morphology and/or protein, breakthrough curves and peaks could be simulated that agreed well with the experimental data while no dependency on either the protein load or the mobile phase composition (salt content) was observed. One of the SMA parameters, namely the characteristic charge needed some slight adjustment (within the error of the experimental determination of this parameter) in order to optimise the fit.
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