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 |
|---|---|
| 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 |
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Keywords
- Barley
- Phospholipid hydroperoxide glutathione peroxidase
- Salt stress
ASJC Scopus subject areas
- Biochemistry
- Catalysis
- Process Chemistry and Technology
Cite this
Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley. / Sugimoto, Manabu; Takeda, Kazuyoshi.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 23, No. 2-6, 01.09.2003, p. 397-403.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure and function of a phospholipid hydroperoxide glutathione peroxidase-like protein from barley
AU - Sugimoto, Manabu
AU - Takeda, Kazuyoshi
PY - 2003/9/1
Y1 - 2003/9/1
N2 - 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.
AB - 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.
KW - Barley
KW - Phospholipid hydroperoxide glutathione peroxidase
KW - Salt stress
UR - http://www.scopus.com/inward/record.url?scp=0041932459&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0041932459&partnerID=8YFLogxK
U2 - 10.1016/S1381-1177(03)00104-8
DO - 10.1016/S1381-1177(03)00104-8
M3 - Article
AN - SCOPUS:0041932459
VL - 23
SP - 397
EP - 403
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
SN - 1381-1177
IS - 2-6
ER -