Preparation and characterisation of surfaces properties of poly(hydroxyethylmethacrylate-co-methacrylolyamido-histidine) membranes:: application for purification of human immunoglobulin G

被引:25
作者
Arica, MY [1 ]
Yalçin, E [1 ]
Bayramoglu, G [1 ]
机构
[1] Kirikkale Univ, Fac Sci, Biochem Proc & Biomat Res Lab, TR-71450 Kirikkale, Turkey
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2004年 / 807卷 / 02期
关键词
poly(hydroxyethylmethacrylate-co-; methacrylolyamido-histidine); immunoglobulin G;
D O I
10.1016/j.jchromb.2004.04.025
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In this study, an affinity membrane containing L-histidine as an amino acid ligand was used in separation and purification of human immunoglobulin G (HIgG) from solution and human serum. The polarities and the surface free energies of the affinity membranes were determined by contact angle measurements. HIgG adsorption and purification onto the affinity membranes from aqueous solution and human serum were investigated in a batch and a continuous system. Effect of different system parameters such as ligand density, adsorbent dosage, pH, temperature, ionic strength and HIgG initial concentration on HIgG adsorption were investigated. The maximum adsorption capacity of p(HEMA-MAAH-4) membranes for HIgG was 13.06 mg ml(-1). The reversible HIgG adsorption on the affinity membrane obeyed both the Langmuir and Freundlich isotherm models. The adsorption data was analysed using the first- and second-order kinetic model and the experimental data was well described by the first-order equations. In the continuous system, the purity of the eluted HIgG, as determined by HPLC, was 93% with recovery 58% for p(HEMA-MAAH-4) membrane. The affinity membranes are stable when subjected to sanitization with sodium hydroxide after repeated adsorption-elution cycles. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:315 / 325
页数:11
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