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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27029

Title: Dehydroascorbate Reductase cDNA from Sweet Potato (Ipomoea batatas [L.] Lam): Expression, Enzyme Properties, and Kinetic Studies
Authors: Yu-Chi Jiang;Chih-Yu Huang;Lisa Wen;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);expression;dehydroascorbate reductase
Date: 2008
Issue Date: 2011-10-21T02:22:22Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract:A cDNA encoding a putative dehydroascorbate reductase (DHAR) was cloned from sweet potato. The deduced protein showed a high level of sequence homology with DHARs from other plants (67 to 81%). Functional sweet potato DHAR was overexpressed and purified. The purified enzyme showed an active monomeric form on a 12% native PAGE. The proteinʼs half-life of deactivation at 50 °C was 10.1 min, and its thermal inactivation rate constant Kd was 6.4 × 10−2 min−1. The enzyme was stable in a broad pH range from 6.0−11.0 and in the presence of 0.8 M imidazole. The Km values for DHA and GSH were 0.19 and 2.38 mM, respectively.
Relation: 56(10), pp.3623–3627
URI: http://ntour.ntou.edu.tw/handle/987654321/27029
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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