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Affinity–based reversed micellar protein extraction: I. Principles and protein–ligand systems
Author(s) -
Kelley Brian D.,
Wang Daniel I. C.,
Hatton T. Alan
Publication year - 1993
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260421010
Subject(s) - chemistry , chromatography , ligand (biochemistry) , micelle , protein purification , amphiphile , octyl glucoside , extraction (chemistry) , aqueous solution , phosphatidylcholine , affinity chromatography , membrane , organic chemistry , biochemistry , enzyme , receptor , phospholipid , copolymer , polymer
Affinity cosurfactants, consisting of hydrophilic ligands derivatized with hydrophobic tails, increase the efficiency of selective protein recoveries using reversed micelles by extending the operating range of pH and salt concentration over which an extraction can be performed. Three different affinity cosurfactant–protein pairs have been used to demonstrate the principles of this extractive technique: (i) concanavalin A, a lectin, was extracted with the addition of octyl glucoside; (ii) natural amphiphiles, such as lecithin, were used to extract myelin basic protein, a membrane‐associated protein known to recognize and bind the phosphatidylcholine headgroup; and (iii) alkyl boronic acids were used to extract chymotrypsin. The enhancement in protein transfer correlated with the binding strength of the free ligand and protein in aqueous solution. Several control studies confirmed the biospecificity of the interactions of protein and affinity cosurfactant. © 1993 John Wiley & Sons, Inc.