Slovak University of Technology, Faculty of Chemical and Food Technology, Institute of Chemical and Environmental Engineering, Department of Chemical and Biochemical Engineering, Radlinského 9, 812 37 Bratislava, Slovakia.
J Chromatogr A. 2011 Sep 28;1218(39):6987-94. doi: 10.1016/j.chroma.2011.07.097. Epub 2011 Aug 6.
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 pK(a) 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.
研究了 pH 值对带有不同配体密度接枝触手层的五组强阳离子交换剂上免疫球蛋白 G、人血清白蛋白和马肌红蛋白的静态吸附容量的影响。对于配体密度较高的吸附剂，观察到吸附容量随 pH 值呈明显的最大值。结果通过蛋白质结构和表面碱性残基可离解基团的 pK(a)计算进行了解释。进行了反尺寸排阻实验，以了解研究蛋白质的吸附容量和孔可及性之间的关系。
