Behavior of human serum albumin on strong cation exchange resins: II. model analysis

Journal of Chromatography. a
Agnes VoitlMassimo Morbidelli

Abstract

Experiments with human serum albumin on a strong cation exchange resin exhibit a peculiar elution pattern: the protein elutes with two peaks in a modifier gradient. This behavior is modeled with a general rate model, where the two elution peaks are modeled with two binding conformations, one of which is at equilibrium conditions, while for the other, the adsorption process is rate limited. Isocratic experiments under nonadsorbing conditions were used to characterize the mass transfer process. The isotherm of both adsorption conformations as well as the kinetic of adsorption and desorption for the second conformation are functions of the modifier concentration. They are evaluated with linear modifier gradient experiments and step experiments with various adsorption times. All experimental features are well reproduced by the proposed modified general rate model.

References

Nov 23, 2006·Journal of Chromatography. a·Emmerich HaimerAlois Jungbauer
Jul 21, 2010·Journal of Chromatography. a·Agnes VoitlMassimo Morbidelli

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Citations

Jul 10, 2012·Journal of Chromatography. a·Ron GillespieSuresh Vunnum
Mar 15, 2011·Journal of Chromatography. a·Wojciech MarekDorota Antos
Jul 21, 2010·Journal of Chromatography. a·Agnes VoitlMassimo Morbidelli
Jan 17, 2021·Journal of Chromatography. a·Linling Yu, Yan Sun

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