AQUEOUS MICELLAR 2-PHASE SYSTEMS FOR PROTEIN SEPARATION

Citation
H. Tani et al., AQUEOUS MICELLAR 2-PHASE SYSTEMS FOR PROTEIN SEPARATION, Analytical sciences, 14(5), 1998, pp. 875-888
Citations number
144
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Chemistry Analytical
Journal title
ISSN journal
0910-6340
Volume
14
Issue
5
Year of publication
1998
Pages
875 - 888
Database
ISI
SICI code
0910-6340(1998)14:5<875:AM2SFP>2.0.ZU;2-F
Abstract
The extractive technique for protein purification based on two-phase s eparation in aqueous micellar solutions (aqueous micellar two-phase sy stem (AMTPS)) is reviewed. The micellar solution of a nonionic surfact ant, such as polyoxyethylene alkyl ether, which is most frequently use d for protein extraction, separates into two phases upon heating above its cloud point. The two phases consist of a surfactant-depleted phas e (aqueous phase) and a surfactant-rich phase. Hydrophilic proteins ar e partitioned to the aqueous phase and hydrophobic membrane proteins a re extracted into the surfactant-rich phase. Because of the methodolog ical simplicity and rapidity, this technique has become an effective m eans, and thus has been widely used for the purification and character ization of proteins. In contrast to polyoxyethylene alkyl ether, micel lar solutions of a zwitterionic surfactant, such as alkylammoniopropyl sulfate, separate below the critical temperature. Alkylglucosides can also separate into two phases upon adding water-soluble polymers. Rec ently, these two-phase systems have been exploited for protein separat ion. Additionally, hydrophobic affinity ligands, charged polymers, and ionic surfactants have been successfully used for controlling the ext ractability of proteins in AMTPS.