Elution relationships to model affinity chromatography using a general rate model
Author
dc.contributor.author
Sandoval, Gabriela
Author
dc.contributor.author
Andrews Farrow, Bárbara
es_CL
Author
dc.contributor.author
Asenjo de Leuze, Juan
es_CL
Admission date
dc.date.accessioned
2014-01-07T13:57:26Z
Available date
dc.date.available
2014-01-07T13:57:26Z
Publication date
dc.date.issued
2012-08-21
Cita de ítem
dc.identifier.citation
J. Mol. Recognit. 2012; 25: 571–579
en_US
Identifier
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DOI: 10.1002/jmr.2223
Identifier
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https://repositorio.uchile.cl/handle/2250/125997
General note
dc.description
Artículo de publicación ISI
en_US
Abstract
dc.description.abstract
Differentmathematicalmodels 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.