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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27066

Title: Monodehydroascorbate Reductase cDNA from Sweet Potato: Expression and Kinetic Studies
Authors: Chih-Yu Huang;Lisa Wen;Rong-Huay Juang;Dey-Chyi Sheu;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
Keywords: Sweet potato Ipomoea batatas L. Lam;3-D homology structure;Expression;Monodehydroascorbate MDAR
Date: 2010-01-01
Issue Date: 2011-10-21T02:22:30Z
Publisher: Botanical Studies
Abstract: Abstract:A cDNA encoding a putative monodehydroascorbate reductase (MDAR) was cloned from sweet potato. The deduced protein showed high level of sequence homology with MDARs from other plants or related family from bacteria (23~80%). A 3-D homology structure was created for this MDAR. Functional sweet potato MDAR was expressed and purified. The purified enzyme showed an active monomeric form on a 10% native PAGE. The protein's half-life of deactivation at 70℃ was 12.4 min, and its thermal inactivation rate constant K(subscript d) was 5.6×10^(-2) min^(-1). The enzyme was stable in a broad pH range from 6.0-10.0, and in the presence of 0.8 M imidazole. The K(subscript m) value for monodehydroascorbate (MDA) and NADH were 21.1 and 39.7 μM, respectively.
Relation: 51(1), pp.37-44
URI: http://ntour.ntou.edu.tw/handle/987654321/27066
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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