Skip to main content
Article
Combination of the steric mass action and non-ideal surface solution models for overload protein ion-exchange chromatography.
Journal of Chromatography A (1997)
  • Poonam Raje
  • Neville G. Pinto, University of Louisville
Abstract
A model has been developed for protein ion-exchange equilibria under overloaded chromatographic conditions. This model combines the steric mass action model with the non-ideal surface solution model and accounts for steric hindrance and nearest neighbor interactions between protein-protein, protein-salt and salt-salt in a single formalism. Using the model on protein ion-exchange data, the importance of obtaining ion-exchange heat measurements in addition to adsorption isotherms has been demonstrated. It has been shown that small inaccuracies in the heat of ion-exchange data can lead to large differences in predictions of elution behavior. Additionally, it has also been shown that salt-salt interactions on the surface can strongly influence protein adsorption and that in the presence of these interactions, the shape and orientation of the molecule on the surface are important.
Keywords
  • Adsorption isotherms,
  • Steric mass action model,
  • Non-ideal surface solution model,
  • Heat of adsorption,
  • Proteins
Disciplines
Publication Date
January, 1997
DOI
10.1016/S0021-9673(96)00812-6
Citation Information
Poonam Raje and Neville G. Pinto. "Combination of the steric mass action and non-ideal surface solution models for overload protein ion-exchange chromatography." Journal of Chromatography A Vol. 760 Iss. 1 (1997) p. 89 - 103 ISSN: 0021-9673
Available at: http://works.bepress.com/neville-pinto/29/