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Bioaffinity separation of trypsin using trypsin inhibitor immobilized in reverse micelles composed of a nonionic surfactant

✍ Scribed by Motonari Adachi; Masaru Yamazaki; Makoto Harada; Aihisa Shioi; Shigeol Katch

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 118 KB
Volume: 53
Category: Article
ISSN: 0006-3592
DOI: 10.1002/(sici)1097-0290(19970220)53:4<406::aid-bit8>3.0.co;2-r

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✦ Synopsis

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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✍ Motonari Adachi; Kengo Shibata; Akihisa Shioi; Makoto Harada; Shigeo Katoh 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 123 KB 👁 2 views

Selective separation of trypsin from a mixture involving many kinds of contaminating proteins, i.e., pancreatin, was achieved using trypsin inhibitor immobilized in the reverse micelles, which were composed of a nonionic surfactant, tetra-oxyethylene monodecylether. To determine the efficient operat