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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27028

Title: Cloning, Expression, and Purification of a Functional Glutathione Reductase from Sweet Potato (Ipomoea batatas [L.] Lam): Kinetic Studies and Characterization
Authors: Cheng-Jen Chen;Chih-Yu Huang;Jenq-Kuen Huang;Choa-Yi Lin;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Sweet potato (Ipomoea batatas [L.] Lam);three-dimensional homology structure (3-D homology structure);expression;glutathione reductase (GR)
Date: 2009
Issue Date: 2011-10-21T02:22:22Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract:A cDNA encoding a putative glutathione reductase (GR) was cloned from sweet potato (Ib). The deduced protein showed high level of sequence homology with GRs from other plants (79−38%). A three-dimensional (3-D) homology structure was created. The active site Cys residues are conserved in all reported GR. Functional IbGR was overexpressed and purified. The purified enzyme showed an active monomeric form on a 10% native polyacrylamide gel electrophoresis (PAGE). The monomeric nature of the enzyme was confirmed by sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDS−PAGE) and molecular mass determination of the native enzyme. The Michaelis constant (Km) values for GSSG (glutathione disulfide) and NADPH (β-nicotinamide adenine dinucleotide phosphate, reduced form) were 0.114 and 0.056 mM, respectively. The enzyme activity was inhibited by Cu2+ and Zn2+, but not by Ca2+. The protein’s half-life of deactivation at 70 °C was 3.3 min, and its thermal inactivation rate constant Kd was 3.48 × 10−1 min−1. The enzyme was active in a broad pH range from 6.0 to 11.0 and in the presence of imidazole up to 0.8 M. The native enzyme appeared to be resistant to digestion by trypsin or chymotrypsin.
Relation: 57(10), pp.4403–4408
URI: http://ntour.ntou.edu.tw/handle/987654321/27028
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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