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Bioaffinity Separation of Trypsin Using Trypsin Inhibitor Immobilized in Reverse Micelles Composed of a Nonionic Surfactant by Motonari Adachi; Masaru Yamazaki; Makoto Harada; Aihisa Shioi; Shigeol Katch is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Bioaffinity Separation of Trypsin Using Trypsin Inhibitor Immobilized in Reverse Micelles Composed of a Nonionic Surfactant about?

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.

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Author

Motonari Adachi; Masaru Yamazaki; Makoto Harada; Aihisa Shioi; Shigeol Katch

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)