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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/32787

Title: A dithiol glutaredoxin cDNA from sweet potato (Ipomoea batatas [L.] Lam): enzyme properties and kinetic studies
Authors: X.-W. Chi;C.-T. Lin;Y.-C. Jiang;L. Wen;C.-T. Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
Keywords: Glutathionylation;sweet potato;three-dimensional structural model (3-D structural model);β-Hydroxyethyl disulphide [HED, (HOCH2CH2)2S2]
Date: 2012-07
Issue Date: 2012-06-18T06:41:37Z
Publisher: Plant Biology
Abstract: Abstract:Glutaredoxins (Grx) play an important role in reduction of protein glutathione mixed disulphides. An IbGrx cDNA (561 bp, EF362614) encoding a putative dithiol Grx was cloned from sweet potato (Ipomoea batatas [L.] Lam). The deduced amino acid sequence is conserved among the reported dithiol Grx, having a CGYC dithiol motif at the active site. A 3-D structural model was created based on the known crystal structure of a poplar Grx (GrxC1). To characterise the IbGrx protein, the coding region was subcloned into an expression vector and transformed into Escherichia coli. The recombinant His6-tagged IbGrx was expressed and purified by metal affinity chromatography. The purified enzyme showed a monomeric band, as demonstrated with 15% SDS-PAGE. The Michaelis constant (KM) for ß-hydroxyethyl disulphide (HED) was 0.50 ± 0.08 Mm. The enzyme retained 60% activity at 80 °C for 16 min. The enzyme was active over a broad pH range from 6.0 to 11.0, and in the presence of imidazole up to 0.4 m. The enzyme was susceptible to protease.
Relation: 14(4), pp.659–665
URI: http://ntour.ntou.edu.tw/handle/987654321/32787
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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