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• W1605036699 abstract "The adsorption behaviour of three anion-exchange sorbents, DEAE Trisacryl M, DEAE Sepharose FF and DEAE Fractogel 650 M has been investigated for proteins of different size and charge distribution. The maximum capacity, qm, and the dissociation constant, Kd, were found to be protein size dependent. Protein loadings with carbonic anhydrase infer unhindered access to the pores of these three sorbents and thus high capacities. Kinetic profiles, monitoring protein uptake from solution, indicated that the rate of adsorption was fast for small proteins. Mathematical models, derived by others, were adopted to extract values for the interaction rate, k1, and the effective diffusion, Dp. The simplest model of Horstmann et al. [J. Chromatogr., 361 (1986) 179] gave high values for k1, confirming that this model lumped together the resistances to mass transfer. Correlation between theory and experiment was best when using the most sophisticated model, that of Arve and Liapis [AIChE. J., 33 (1987) 179] where the resulting values for k1 were larger. Diffusion for the smaller proteins agreed well with bulk diffusion, indicating little restriction to mass transfer through the pores. Contrary to this, values of Dp for the largest protein, ferritin, were 1 /40th of the free diffusivities, further highlighting the influence of protein size on pore accessibility." @default.
• W1605036699 created "2016-06-24" @default.
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• W1605036699 date "1991-09-01" @default.
• W1605036699 modified "2023-10-16" @default.
• W1605036699 title "High-performance liquid chromatography of amino acids, peptides and proteins" @default.
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• W1605036699 doi "https://doi.org/10.1016/s0021-9673(01)87143-0" @default.
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