Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1201815 | Journal of Chromatography A | 2011 | 8 Pages |
Abstract
The effect of pH on the static adsorption capacity of immunoglobulin G, human serum albumin, and equine myoglobin was investigated for a set of five strong cation exchangers with the grafted tentacle layer having a different ligand density. A sharp maximum of adsorption capacity with pH was observed for adsorbents with a high ligand density. The results were elucidated using the protein structure and calculations of pKa of ionizable groups of surface basic residues. Inverse size-exclusion experiments were carried out to understand the relation between the adsorption capacity and pore accessibility of the investigated proteins.
Related Topics
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Analytical Chemistry
Authors
Katarzyna Wrzosek, Milan Polakovič,