Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.
Original languageEnglish
Pages (from-to)176-185
Number of pages10
JournalArchives of Biochemistry and Biophysics
Publication statusPublished - 1987


  • Alkaline Phosphatase
  • Antioxidants
  • Ascorbic Acid
  • Catalase
  • Cations, Divalent
  • Copper
  • Ferric Compounds
  • Ferrous Compounds
  • Free Radicals
  • Glutathione
  • Hydrogen Peroxide
  • Hydroxides
  • Hydroxyl Radical
  • Kinetics
  • Mercaptoethanol
  • Metals
  • Mixed Function Oxygenases
  • Oxidation-Reduction
  • Peroxidase
  • Superoxide Dismutase
  • Thiourea
  • Uric Acid
  • Vitamin E
  • Xanthine Oxidase


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