Affinity membrane chromatography for the analysis and purification of proteins

Citation
Hf. Zou et al., Affinity membrane chromatography for the analysis and purification of proteins, J BIOCH BIO, 49(1-3), 2001, pp. 199-240
Citations number
166
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
ISSN journal
0165022X → ACNP
Volume
49
Issue
1-3
Year of publication
2001
Pages
199 - 240
Database
ISI
SICI code
0165-022X(20011030)49:1-3<199:AMCFTA>2.0.ZU;2-#
Abstract
Affinity chromatography is unique among separation methods as it is the onl y technique that permits the purification of proteins based on biological f unctions rather than individual physical or chemical properties. The high s pecificity of affinity chromatography is due to the strong interaction betw een the ligand and the proteins of interest. Membrane separation allows the processing of a large amount of sample in a relatively short time owing to its structure, which provides a system with rapid reaction kinetics. The i ntegration of membrane and affinity chromatography provides a number of adv antages over traditional affinity chromatography with porous-bead packed co lumns, especially with regard to time and recovery of activity. This review gives detailed descriptions of materials used as membrane substrates, prep aration of basic membranes, coupling of affinity ligands to membrane suppor ts, and categories of affinity membrane cartridges. It also summarizes the applications of cellulose/glycidyl methacrylate composite membranes for pro teins separation developed in our laboratory. (C) 2001 Elsevier Science B.V . All rights reserved.