Purification and characterization of a novel monomeric glutathione peroxidase from rat liver.

@article{Duan1988PurificationAC,
  title={Purification and characterization of a novel monomeric glutathione peroxidase from rat liver.},
  author={Yun-biao Duan and Sadaaki Komura and Berta Fiszer-Szafarz and D. Szafarz and Kunio Yagi},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 35},
  pages={19003-8}
}
A novel glutathione peroxidase, which is active toward hydroperoxides of phospholipid in the presence of a detergent, has been purified to homogeneity from a rat liver postmicrosomal supernatant fraction by ammonium sulfate fractionation and three different column chromatographies. From a DE52 column, glutathione peroxidase active toward phosphatidylcholine dilinoleoyl hydroperoxides was eluted in one major and two minor peaks. The enzyme in the major peak was found to be separated from the… CONTINUE READING