作者: Graham L. Skidmore , Brenda J. Hortsmann , Howard A. Chase
DOI: 10.1016/S0021-9673(01)84240-0
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摘要: Abstract The equilibrium and kinetic characteristics of the adsorption bovine serum albumin (BSA) lysozyme to strong cation exchanger S Sepharose FF have been determined. rates protein compared two different models, first being based on a single lumped parameter, whilst second model considers individual transport processes occurring prior reaction, that is taking into account diffusion across liquid film surrounding particles also within ion-exchanger particle itself. It was found FF, in both batch, agitated tanks packed beds consistent with models. In case BSA however, tank profile only pore neither correctly predicted latter part breakthrough observed packed-bed experiments.