NADH oxidase activity of human xanthine oxidoreductase--generation of superoxide anion.

@article{Sanders1997NADHOA,
  title={NADH oxidase activity of human xanthine oxidoreductase--generation of superoxide anion.},
  author={S. Sanders and R. Eisenthal and R. Harrison},
  journal={European journal of biochemistry},
  year={1997},
  volume={245 3},
  pages={
          541-8
        }
}
  • S. Sanders, R. Eisenthal, R. Harrison
  • Published 1997
  • Biology, Medicine
  • European journal of biochemistry
  • Human xanthine oxidase was purified from breast milk. The dehydrogenase form of the enzyme, which predominates in most mammalian tissues, catalyses the oxidation of NADH by oxygen, generating superoxide anion significantly faster than does the oxidase form. The corresponding forms of bovine enzyme behave very similarly. The steady-state kinetics of NADH oxidation and superoxide production, including inhibition by NAD, by the dehydrogenase forms of both enzymes, are analysed in terms of a model… CONTINUE READING
    The thermodynamics of xanthine oxidoreductase catalysis.
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