期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1218, 期 39, 页码 6987-6994出版社
ELSEVIER
DOI: 10.1016/j.chroma.2011.07.097
关键词
Cation-exchange chromatography; Grafted tentacle layer; Protein adsorption capacity; Ligand density; pH influence; Surface residues; Ionization
资金
- EU [NMP3-CT-2004-500160]
- Slovak Grant Agency for Science, VEGA [1/0655/09]
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. (C) 2011 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据