This article is published in Journal of Molecular Recognition as part of the special issue on Affinity 2011 - The 19th biennial meeting of the International Society for Molecular Recognition, edited by Gideon Fleminger (Tel-Aviv University, Israel) and George Ehrlich (Hoffmann-La Roche, Nutley, NJ).
Special Issue Article
Elution relationships to model affinity chromatography using a general rate model†
Version of Record online: 29 OCT 2012
Copyright © 2012 John Wiley & Sons, Ltd.
Journal of Molecular Recognition
Special Issue: Affinity 2011 – The 19th biennial meeting of the International Society for Molecular Recognition
Volume 25, Issue 11, pages 571–579, November 2012
How to Cite
Sandoval, G., Andrews, B. A. and Asenjo, J. A. (2012), Elution relationships to model affinity chromatography using a general rate model. J. Mol. Recognit., 25: 571–579. doi: 10.1002/jmr.2223
- Issue online: 24 OCT 2012
- Version of Record online: 29 OCT 2012
- Manuscript Accepted: 21 AUG 2012
- Manuscript Revised: 20 AUG 2012
- Manuscript Received: 13 JAN 2012
- affinity chromatography;
- rate model;
- elution (adsorption/desorption) relationships
Different mathematical models with different degrees of complexity have been proposed to model affinity chromatography. In this work, in particular, a general rate model has been studied that considers axial dispersion, external film mass transfer, intraparticle diffusion, and kinetic effects investigating the influence in the simulations of two different relationships between the properties of the mobile phase and the affinity of different proteins to the ligand bound to the matrix. Two systems were used: Blue Sepharose and Protein A. With Blue Sepharose, an increasing linear salt gradient was used, and with Protein A, a decreasing semi-linear pH gradient. The kinetic parameters obtained in each of the two elution (adsorption/desorption) relationships studied (a power law type and an exponential type) led to very good agreements between experimental and simulated elution curves of mixtures of proteins finding that for more symmetrical peaks, the preferred elution relationship should be the exponential one, in contrast to the more asymmetrical peaks which shapes are better simulated by the power law relationship. Copyright © 2012 John Wiley & Sons, Ltd.