Selective purification of intestinal maltase complex by affinity chromatography employing an uncompetitive inhibitor as the ligand


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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/58487

Title:	Selective purification of intestinal maltase complex by affinity chromatography employing an uncompetitive inhibitor as the ligand
Authors:	Kato, Eisuke Browse this author →KAKEN DB
	Tsuji, Hiroki Browse this author
	Kawabata, Jun Browse this author →KAKEN DB
Keywords:	Affinity chromatography
	Uncompetitive inhibitor
	Glucosidase inhibitor
	Intestinal glucosidase
	Maltase-glucoamylase complex
Issue Date:	4-Mar-2015
Publisher:	Elsevier
Journal Title:	Tetrahedron
Volume:	71
Issue:	9
Start Page:	1419
End Page:	1424
Publisher DOI:	10.1016/j.tet.2015.01.019
Abstract:	Affinity chromatography of specific enzymes is limited by the presence of related enzymes and the limited selectivity of the affinity ligand. We synthesized and investigated the use of an uncompetitive inhibitor as an affinity ligand, to leverage its three-component interactions. Use of the potent α-glucosidase uncompetitive inhibitor 2-aminoresorcinol as the ligand of the affinity gel offered selective purification of maltase-glucoamylase complex from the crude mixture of intestinal α-glucosidases.
Type:	article (author version)
URI:	http://hdl.handle.net/2115/58487
Appears in Collections:	農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 加藤英介

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