Binary Adsorption Processes of Albumin and Immunoglobulin on Hydrophobic Charge-Induction Resins

被引：12
作者：
Zhang, Qilei [1 ]
Schimpf, Ferdinand [1 ,2 ]
Lu, Hui-Li [1 ]
Lin, Dong-Qiang [1 ]
Yaot, Shan-Jing [1 ]
机构：
[1] Zhejiang Univ, Dept Chem & Biol Engn, Key Lab Biomass Chem Engn, Minist Educ, Hangzhou 310027, Zhejiang, Peoples R China
[2] Tech Univ Munich, Inst Biochem Engn, D-85748 Garching, Germany
来源：
JOURNAL OF CHEMICAL AND ENGINEERING DATA | 2016年 / 61卷 / 03期
基金：
中国国家自然科学基金;
关键词：
COMPETITIVE PROTEIN ADSORPTION; LASER-SCANNING MICROSCOPY; ION-EXCHANGE MEDIA; ANTIBODY PURIFICATION; CONFOCAL MICROSCOPY; POLYMER SURFACES; IGG PURIFICATION; CHROMATOGRAPHY; KINETICS; DISPLACEMENT;
D O I：
10.1021/acs.jced.5b01108
中图分类号：
O414.1 [热力学];
学科分类号：
摘要：
Hydrophobic charge-induction chromatography with 4-mercaptoethyl-pyridine as ligands shows promising application in antibody purification. In this study, competitive adsorption of protein mixtures composed with bovine serum albumin (BSA) and immunoglobulin (IgG) was investigated with MEP HyperCel. Static adsorption and dynamic binding processes were measured under different media pH and BSA/IgG mass ratios. The results showed that MEP HyperCel had high pH-dependent selectivity. BSA can be adsorbed quicker than IgG but part of the adsorbed BSA would be gradually displaced by IgG as a result of competitive adsorption. The effects of NaCI and (NH4)(2)SO4 on protein mixture adsorption showed that both salts can enhance IgG selectivity on MEP HyperCel, but the effect was different based on the combination of electrostatic and hydrophobic interactions. Competitive adsorption mechanism was discussed and the results obtained would be useful in the separation of albumin and immunoglobulin from protein mixtures.
引用
收藏
页码：1353 / 1360
页数：8
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