Oxidation of glutathione by the myeloperoxidase system.

@article{Turkall1982OxidationOG,
  title={Oxidation of glutathione by the myeloperoxidase system.},
  author={Rita M. Turkall and Min-fu Tsan},
  journal={Journal of the Reticuloendothelial Society},
  year={1982},
  volume={31 4},
  pages={353-60}
}
Oxidation of glutathione (GSH) by the myeloperoxidase (MPO) system was studied. The combination of MPO, H2O2, and a halide ion oxidized GSH. This occurred at a H2O2 concentration too low to oxidize GSH by itself. The MPO-mediated oxidation of GSH required the simultaneous presence of MPO, H2O2, and a halide ion. The system had an acid pH optimum of pH 5.5-6.0. Iodide was more effective than bromide which in turn was more effective than chloride. The oxidative product was shown to be GSSG, since… CONTINUE READING