EFFICIENT RECOVERY OF RECOMBINANT PROTEINS USING MEMBRANE-BASED IMMUNOAFFINITY CHROMATOGRAPHY (MIC)

被引：26

作者：

NACHMAN, M ^{[1
]}

AZAD, ARM ^{[1
]}

BAILON, P ^{[1
]}

机构：

[1] SEPRACOR INC,MARLBOROUGH,MA 01752

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 1992年 / 40卷 / 05期

关键词：

MEMBRANES; IMMUNOAFFINITY; RECOMBINANT; INTERFERON; INTERLEUKIN-2; RECEPTOR;

D O I：

10.1002/bit.260400503

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A systematic approach to the design and development of membrane-based immunoaffinity systems for the purification of recombinant proteins is presented. The preparation and characterization of immunoaffinity membranes are described. The immunoaffinity purification process for recombinant interferon-alpha-2a is used as a model system to determine the operational parameters in membrane-based immunoaffinity chromatography. The high volumetric throughput of membranes, combined with the typically fast-binding kinetics of antigen-antibody interactions, enable the purification of recombinant proteins from dilute feed stream in less time, using less antibody than conventional systems. Three recombinant proteins, human interferon-alpha-2a, interleukin-2, and interleukin-2 receptor, have been purified efficiently employing membrane-based immunoaffinity chromatography. Overall, membrane-based immunoaffinity chromatography is shown to be a viable and scalable method, ideal for the industrial-scale production of recombinant proteins.

引用

页码：564 / 571

页数：8

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