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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27068

Title: Putative phospholipid hydroperoxide glutathione peroxidase from Antrodia camphorata
Authors: Hsueh-Tai Chen;Choa-Yi Lin;Chuian-Fu Ken;Lisa Wen;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
Keywords: Antrodia camphorata;Antioxidation;Phospholipid hydroperoxide glutathione peroxidase (PHGPx);Taiwanofungus
Date: 2009-07-15
Issue Date: 2011-10-21T02:22:30Z
Publisher: Food Chemistry
Abstract: Abstract:Glutathione Peroxidases (GPxs) play important roles in antioxidation. A cDNA (Ac-PHGPx, 764 bp) encoding a putative phospholipid hydroperoxide glutathione peroxidase (PHGPx) from Antrodia camphorata has been cloned. The deduced amino acid sequence is conserved among the reported GPxs. To characterize the Ac-PHGPx, the coding region was subcloned into pYEX-S1 and transformed into Saccharomyces cerevisiae. The recombinant 6His-tagged Ac-PHGPx was expressed and purified by Ni2+-nitrilotriacetic acid Sepharose. The purified enzyme showed a predominant band with molecular mass of ∼18 kDa on 12% SDS–PAGE. The enzyme retained 50% activity at 60 °C for 8 min. The enzyme was most active at pH 9. The enzyme showed 42% activity after incubation with trypsin at 37 °C for 40 min. In addition, the ability of Ac-PHGPx to protect intact supercoiled plasmid DNA from OH induced nicking was demonstrated.
Relation: 115(2), pp.476–482
URI: http://ntour.ntou.edu.tw/handle/987654321/27068
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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