National Changhua University of Education Institutional Repository : Item 987654321/16779

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NCUEIR > College of Science > Department of Biology > Periodical Articles > Item 987654321/16779

Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/16779

Title:	Putative Phospholipid Hydroperoxide Glutathione Peroxidase from Antrodia Camphorate
Authors:	Chen, Hsueh-Tai;Lin, Choa-Yi;Ken, Chuian-Fu;Wen, Lisa;Lin, Chi-Tsai
Contributors:	生物學系
Keywords:	Antrodia camphorata;Antioxidation;Phospholipid hydroperoxide glutathione peroxidase (PHGPx);Taiwanofungus
Date:	2009-07
Issue Date:	2013-06-05T08:48:21Z
Publisher:	Elsevier
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:	Food Chemistry, 115(2): 476-482
Appears in Collections:	[Department of Biology] Periodical Articles

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