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Influence of lateral interactions on preparative protein chromatography : I. Isotherm behavior.
Journal of Chromatography A (1994)
  • Yong-Long Li
  • Neville G. Pinto, University of Louisville
A thermodynamically consistent adsorption equilibrium model based on the stoichiometric displacement principle has been developed for non-linear protein ion exchange. The adsorbed phase is modeled as a surface solution in equilibrium with an ideal bulk liquid, and non-idealities on the surface are calculated from surface activity coefficients. The model has been used to systematically investigate the influence of lateral interactions on equilibrium isotherms. Using experimental data for the ion exchange of bovine serum albumin, it has been shown that lateral interactions are a function of the adsorbed protein concentration, and this dependence strongly influences adsorption behavior. Lateral interactions on the surface have been found to be influenced by both energy of interactions between molecules and molecular shape, with the former being dominant. The relationships between lateral interactions, effective protein charge, and modulator concentration have also been investigated. Increases in adsorbate charge may result in an increase or decrease in adsorption capacity, depending on the relative concentration of the modulator, while increases in modulator concentration decrease capacity. For a complete characterization of salt effects, it is necessary to determine the dependence of isosteric heat of adsorption on salt concentration.
Publication Date
January, 1994
Citation Information
Yong-Long Li and Neville G. Pinto. "Influence of lateral interactions on preparative protein chromatography : I. Isotherm behavior." Journal of Chromatography A Vol. 658 Iss. 2 (1994) p. 445 - 457
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