Peroxidase properties of extracellular superoxide dismutase: role of uric acid in modulating in vivo activity.

@article{Hink2002PeroxidasePO,
  title={Peroxidase properties of extracellular superoxide dismutase: role of uric acid in modulating in vivo activity.},
  author={H Ulrich Hink and Nalini Santanam and Sergey I. Dikalov and Louise A. McCann and Andrew D Nguyen and Sampath Parthasarathy and David G Harrison and Tohru Fukai},
  journal={Arteriosclerosis, thrombosis, and vascular biology},
  year={2002},
  volume={22 9},
  pages={1402-8}
}
OBJECTIVE The cytosolic form of Cu/Zn-containing superoxide dismutase (SOD1) has peroxidase activity, with H2O2 used as a substrate to oxidize other molecules. We examined peroxidase properties of the extracellular form of SOD (SOD3), a major isoform of SOD in the vessel wall, by using recombinant SOD3 and an in vivo model of atherosclerosis. METHODS AND RESULTS In the presence of HCO3-, SOD3 reacted with H2O2 to produce a hydroxyl radical adduct of the spin trap 5-diethoxyphosphoryl-5methyl… CONTINUE READING
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