Loading...
|
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: | [生物學系] 期刊論文
|
Files in This Item:
| File |
Size | Format | |
|---|
| index.html | 0Kb | HTML | 538 | View/Open |
|
All items in NCUEIR are protected by copyright, with all rights reserved.
|
