Putative phospholipid hydroperoxide glutathione peroxidase from Antrodia camphorata

Hsueh T. Chen, Choa Y. Lin, Chuian-Fu Ken, Lisa Wen, Chi Tsai Lin

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11 Citations (Scopus)

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 {radical dot}OH induced nicking was demonstrated.

Original languageEnglish
Pages (from-to)476-482
Number of pages7
JournalFood Chemistry
Volume115
Issue number2
DOIs
Publication statusPublished - 2009 Jul 15

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All Science Journal Classification (ASJC) codes

  • Food Science
  • Analytical Chemistry

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