Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley

Manabu Sugimoto, Kazuyoshi Takeda

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)

    Abstract

    A cDNA encoding barley phospholipid hydroperoxide glutathione peroxidase (PHGPX)-like protein was cloned and sequenced by the reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends methods. The cDNA comprised 846bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,532Da. The deduced amino acid sequence showed significant identity to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to produce an extra protein, which showed a molecular mass similar to the deduced one, and the clone cells were much more tolerant to NaCl stress than the host cells.

    Original languageEnglish
    Pages (from-to)397-403
    Number of pages7
    JournalJournal of Molecular Catalysis B: Enzymatic
    Volume23
    Issue number2-6
    DOIs
    Publication statusPublished - Sep 1 2003

    Keywords

    • Barley
    • Phospholipid hydroperoxide glutathione peroxidase
    • Salt stress

    ASJC Scopus subject areas

    • Catalysis
    • Bioengineering
    • Biochemistry
    • Process Chemistry and Technology

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