학술논문

Determination of [beta]-glucosidase aggregating factor (BGAF) binding and polymerization regions on the maize [beta]-glucosidase isozyme Glu1
Document Type
Report
Source
Phytochemistry. July-August, 2009, Vol. 70 Issue 11-12, p1355, 11 p.
Subject
Hydrolases -- Chemical properties
Enzymes -- Chemical properties
Lectins -- Chemical properties
Corn -- Chemical properties
Liquid chromatography -- Chemical properties
Polymerization -- Chemical properties
Language
English
ISSN
0031-9422
Abstract
To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.phytochem.2009.07.026 Byline: Hyun Young Yu (a), Farooqahmed S. Kittur (a), David R. Bevan (b), Asim Esen (a) Keywords: [beta]-Glucosidase; [beta]-Glucosidase aggregating factor (BGAF); Protein-protein interaction; Binding site; Gel-shift assay; Pull-down assay; Frontal affinity chromatography (FAC) Abbreviations: 4-MUGlc, 4-methylumbelliferyl-[beta]-d-glucoside; BGAF, [beta]-glucosidase aggregating factor; Dhr1, sorghum [beta]-glucosidase isozyme Dhr1; Dhr2, sorghum [beta]-glucosidase isozyme Dhr2; DIMBOAGlc, 2-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one; FAC, frontal affinity chromatography; Glu1, maize [beta]-glucosidase isozyme Glu1; IPTG, isopropyl [beta]-d-1-thiogalactopyranoside; JRL, jacalin-related lectin; PBS, phosphate-buffered saline; PCR, polymerase chain reaction; pNPGlc, p-nitrophenyl-[beta]-d-glucoside; HPLC, high performance liquid chromatography Abstract: This study defines the regions that contribute to the [beta]-glucosidase aggregating factor (BGAF) binding site of the maize [beta]-glucosidase isozyme Glu1 and provides insights into the mechanism of Glu1-BGAF interaction. Author Affiliation: (a) Department of Biological Sciences, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0406, USA (b) Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA Article History: Received 18 March 2009; Revised 1 June 2009; Accepted 23 July 2009