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 language | English |
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Pages (from-to) | 397-403 |
Number of pages | 7 |
Journal | Journal of Molecular Catalysis B: Enzymatic |
Volume | 23 |
Issue number | 2-6 |
DOIs | |
Publication status | Published - Sep 1 2003 |
Keywords
- Barley
- Phospholipid hydroperoxide glutathione peroxidase
- Salt stress
ASJC Scopus subject areas
- Catalysis
- Bioengineering
- Biochemistry
- Process Chemistry and Technology