Covalent Chromatography for Chymotrypsin-like Proteases Using a Diphenyl 1-Amino-2-phenylethylphosphonate Derivative
-
- Ono Shin
- Graduate School of Science and Engineering, University of Toyama
-
- Murai Junya
- Graduate School of Science and Engineering, University of Toyama
-
- Furuta Seigo
- Graduate School of Science and Engineering, University of Toyama
-
- Doike Kazuya
- Graduate School of Science and Engineering, University of Toyama
-
- Manzaki Fumie
- Graduate School of Science and Engineering, University of Toyama
-
- Yoshimura Toshiaki
- Graduate School of Science and Engineering, University of Toyama
-
- Kuroda Hirofumi
- Department of Applied Chemistry and Chemical Engineering, Toyama National College of Technology
-
- Umezaki Masahito
- Institute of Natural Medicine, University of Toyama
-
- Oyama Hiroshi
- Faculty of Science and Engineering, Setsunan University
この論文をさがす
説明
To establish a covalent chromatography system for purification of naturally occurring chymotrypsin-like serine proteases, a diphenyl 1-amino-2-phenylethylphosphonate derivative bearing Gly-Gly-Gly as a spacer was immobilized on the Sepharose 4FF gel. In this system, bovine chymotrypsin was selectively bound to the phosphonate immobilized on the gel and then released by the action of 2-pyridinealdoxime methiodide as the reactivated enzyme. Based on the study results for selective binding and reactivation conditions, chymotrypsin-like proteases from pancreatin (hog pancreas) were rapidly and highly purified within three hours.
収録刊行物
-
- Journal of Biological Macromolecules
-
Journal of Biological Macromolecules 13 (3), 78-85, 2013
日本生物高分子学会