Corpus ID: 29074173

The formation of styrene glutathione adducts catalyzed by prostaglandin H synthase. A possible new mechanism for the formation of glutathione conjugates.

@article{Stock1986TheFO,
  title={The formation of styrene glutathione adducts catalyzed by prostaglandin H synthase. A possible new mechanism for the formation of glutathione conjugates.},
  author={Byron Stock and John Richard Bend and Thomas E. Eling},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 13},
  pages={
          5959-64
        }
}
  • Byron Stock, John Richard Bend, Thomas E. Eling
  • Published 1986
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • The metabolism of styrene by prostaglandin hydroperoxidase and horseradish peroxidase was examined. Ram seminal vesicle microsomes in the presence of arachidonic acid or hydrogen peroxide and glutathione converted styrene to glutathione adducts. Neither styrene 7,8-oxide nor styrene glycol was detected as a product in the incubation. Also, the addition of styrene 7,8-oxide and glutathione to ram seminal vesicle microsomes did not yield styrene glutathione adducts. The peroxidase-generated… CONTINUE READING