シロイヌナズナ由来過酸化リン脂質グルタチオンペルオキシダーゼ様遺伝子のクローニングと発現

A cDNA encoding Arabidopsis purative phosphplipid hydroperoxide gultathione peroxidase (PHGPX) was cloned and sequenced by the reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends methods. The cDNA comprised 803 bp, and included an open reading frame which encodes a polypeptide of 169 amino acid residues with a molecular mass of 18,600 Da. The deduced amino acid sequence showed homology to plant putative PHGPXs and mammalian PHGPXs. The cloned gene was expressed in Escherichia coli cells to prouce an extra protein, which showed a molecular mass similar to the deduced one.