Behavior of human serum albumin on strong cation exchange resins: II. model analysis.
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.
Voitl
Agnes
A
Institute for Chemical and Bioengineering, Department of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zurich, Switzerland.
Butté
Alessandro
A
Morbidelli
Massimo
M
D000327:Adsorption; D002411:Cation Exchange Resins / Q000737:chemistry*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D003198:Computer Simulation; D006801:Humans; D007700:Kinetics; D008962:Models, Theoretical; D016062:Porosity; D011485:Protein Binding; D012044:Regression Analysis; D012709:Serum Albumin / Q000737:chemistry*; D013696:Temperature
D002411:Cation Exchange Resins; D012709:Serum Albumin