Molecular Cloning and Characterization of a cDNA Encoding Putative Phospholipid Hydroperoxide Glutathione Peroxidase from Spinach
Author(s) -
Manabu Sugimoto,
Satoshi Furui,
Yukio Suzuki
Publication year - 1997
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.61.1379
Subject(s) - spinach , phospholipid hydroperoxide glutathione peroxidase , complementary dna , open reading frame , biochemistry , biology , molecular cloning , peptide sequence , gene , gpx6 , amino acid , peroxidase , cloning (programming) , microbiology and biotechnology , gpx3 , arabidopsis , glutathione peroxidase , glutathione , enzyme , computer science , mutant , programming language
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.
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