Comparison of protein A affinity sorbents II. Mass transfer properties

被引:135
作者
Hahn, R [1 ]
Bauerhansl, P [1 ]
Shimahara, K [1 ]
Wizniewski, C [1 ]
Tscheliessnig, A [1 ]
Jungbauer, A [1 ]
机构
[1] Univ Nat Resources & Appl Life Sci, Dept Biotechnol, A-1190 Vienna, Austria
关键词
Staphylococcus protein A; antibody; immunoglobulin; pore diffusion; film diffusion;
D O I
10.1016/j.chroma.2005.07.050
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Protein A affinity chromatography is the standard purification method for isolation of therapeutic antibodies. Due to improvements in expression technology and optimization of fermentation, culture supernatants with high antibody content must be processed. Recently protein A affinity media with improved adsorption characteristics have been developed. The agarose media MabSelect Xtra and MabSelect SuRe are recent developments of the existing protein A affinity medium MabSelect. MabSelect Xtra is designed to exhibit a higher binding capacity for IgG, and MabSelect SuRe is functionalized with an alkaline stabilized protein A. ProSep-vA Ultra is a porous glass medium with a pore size of 70 nm, also developed to improve the binding capacity. Adsorption was measured in a finite and infinite bath. Mass transfer in these systems could be well described by a model including film and pore diffusion. Mass transfer parameters were used to accurately predict IgG breakthrough in packed bed mode. The dynamic binding capacity of all three media did not change when residence time was at least 4 min. All three media are suited for capture of feed stocks with high antibody content. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:98 / 110
页数:13
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