Comparison of antibody binding to immobilized group specific affinity ligands in high performance monolith affinity chromatography

被引:64
作者
Berruex, LG
Freitag, R [1 ]
Tennikova, TB
机构
[1] Swiss Fed Inst Technol, Ctr Biotechnol, Inst Chem Engn, CH-1015 Lausanne, Switzerland
[2] Russian Acad Sci, Inst Macromol Cpds, St Petersburg 199004, Russia
关键词
high performance monolith affinity chromatography; antibodies; immobilized group specific ligands;
D O I
10.1016/S0731-7085(00)00414-3
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
A novel biochromatographic principle is introduced taking the quantitative analysis of affinity interactions between antibodies and immobilized group specific ligands (protein A, G, and L) as example. The name high performance monolith affinity chromatography (HPMAC) is proposed for this technique. HPMAC uses rigid, macroporous monoliths, so-called convective interaction media (CIM(TM))-disks, as stationary phase. An optimized procedure is described for the covalent immobilization of the group specific affinity ligands to such disks. The binding of polyclonal bovine Ige and a recombinant human antibody (type IgG1-kappa) to all affinity disks is discussed. An essential feature of HPMAC is its compatibility to unusually high mobile phase flow rates (> 4 ml/min). Chromatographic experiments are thus completed within seconds without significant loss in binding capacity and retentive power. This makes HPMAC a promising tool for applications in fast process monitoring or screening. As an example for the former, the direct quantitative isolation of recombinant antibodies from serum-free culture supernatant is demonstrated. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:95 / 104
页数:10
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