Abstract
The high-performance ion-exchange gradient-elution behaviour of a range of globular proteins has been investigated, using a strong anion exchanger as the stationary phase and sodium chloride as the displacer salt. Deviations were observed between the Z c values obtained from isocratic experiments and from gradient experiments with varied gradient time and varied flow-rate. These results indicate that theoretical treatments which relate gradient and isocratic elution processes do not adequately describe the retention behaviour of protein solutes separated by ion-exchange methods. Furthermore, the experimentally observed bandwidths deviated significantly from values predicted on the basis of plate theory for low-molecular-weight molecules. The significance of these results is discussed in terms of the influence of experimental parameters on the ability of particular electrostatically interactive areas on the surface of protein solutes to control the thermodynamic and kinetic properties of these polyelectrolyte molecules during ion-exchange chromatographic processes.
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