title: Bioaffinity separation of trypsin using trypsin inhibitor immobilized in reverse micelles composed of a nonionic surfactant.
abstract: Trypsin inhibitor was converted to hydrophobic states by covalently combining cholesteryl groups using an acylation reaction, and was immobilized in reverse micelles composed of a nonionic surfactant. Using this reverse micellar phase containing trypsin inhibitor as an affinity ligand, trypsin was selectively separated with high recoveries from a mixture of several kinds of contaminating proteins by forward and backward extraction. No loss of activity of the recovered trypsin was observed through these operations. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 406-408, 1997.
authors.affiliation: Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Adachi
authors.forename: M
authors.initials: M
authors.lastname: Yamazaki
authors.forename: M
authors.initials: M
authors.lastname: Harada
authors.forename: A
authors.initials: A
authors.lastname: Shioi
authors.forename: S
authors.initials: S
authors.lastname: Katch