Molecular cloning and characterization of a cDNA encoding putative phospholipid hydroperoxide glutathione peroxidase from spinach.

Manabu Sugimoto, S. Furui, Y. Suzuki

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

A cDNA encoding spinach putative phospholipid hydroperoxide glutathione peroxidase (PHGPX) was cloned and sequenced. The cDNA included an open reading frame that encoded a polypeptide of 171 amino acid residues. The deduced amino acid sequence showed about 77 and 50% similarity to plant putative PHGPXs and mammalian PHGPXs, respectively. PCR product with the same size as that of the spinach putative PHGPX were obtained from maize, soybeans, and Arabidopsis, suggesting the expression of putative PHGPX genes in other plants.

Original languageEnglish
Pages (from-to)1379-1381
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume61
Issue number8
Publication statusPublished - Aug 1997

Fingerprint

phospholipid-hydroperoxide glutathione peroxidase
Spinacia oleracea
Cloning
Phospholipids
Molecular Cloning
spinach
molecular cloning
Complementary DNA
Amino acids
Amino Acids
Polypeptides
Soybeans
Arabidopsis
Open Reading Frames
Zea mays
Amino Acid Sequence
Genes
Polymerase Chain Reaction
Peptides
open reading frames

ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

Cite this

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