國家衛生研究院 NHRI:Item 3990099045/3954
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    题名: Cloning, expression, and characterization of an enzyme possessing both glutaredoxin and dehydroascorbate reductase activity from taiwanofungus camphorata
    作者: Ken, CF;Lin, CY;Jiang, YC;Wen, L;Lin, CT
    贡献者: National Institute of Cancer Research
    摘要: Glutaredoxins (Grxs) play important roles in the reduction of disulfides via reduced glutathione as a reductant. A cDNA (503 bp, EU 193660) encoding a putative Grx was cloned from Taiwanofugus camphorata (Tc). The deduced amino acid sequence is conserved among the reported dithiol Grxs. A 3D homology structure was created for this TcGrx. To characterize the TcGrx enzyme, the coding region was subcloned into an expression vector pET-20b(+) and transformed Into Escherichia coli. Functional TcGrx was expressed and purified by Ni 2+-nitrllotriacetic acid Sepharose. The purified enzyme showed bands of ?15 kDa on 15% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The TcGrx encodes a protein possessing both Grx and dehydroascorbate reductase (DHAR) activity. The Michaelis constant (Km) values for β-hydroxyethyl disulfide (HED) and dehydroascorbate (DHA) were 0.57 and 1.85 mM, respectively. The half-life of deactivation of the protein at 100 °C was 8.5 min, and its thermal inactivation rate constant Kd was 6.52 x 10-2 min-1. The enzyme was active under a broad pH range from 6.0 to 10.0 and in the presence of imidazole up to 0.4 M. The enzyme was susceptible to SDS denaturation and protease degradation/inactivation.
    日期: 2009-11-11
    關聯: Journal of Agricultural and Food Chemistry. 2009 Nov 11;57(21):10357-10362.
    Link to: http://dx.doi.org/10.1021/jf9021256
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0021-8561&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000271290800068
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=70449101120
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