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Alkaline phosphatase inactivation by mixed function oxidation systems.

A Mordente1, G A Miggiano, G E Martorana

  • 1Istituto di Chimica Biologica, Università Cattolica del S. Cuore Facoltà di Medicina e Chirurgia Agostino Gemelli, Roma, Italy.

Archives of Biochemistry and Biophysics
|October 1, 1987
PubMed
Summary
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Alkaline phosphatase inactivation is caused by hydroxyl radicals, which damage the enzyme near its active site. Uric acid effectively protects the enzyme, unlike Vitamin E.

Area of Science:

  • Biochemistry
  • Enzymology
  • Oxidative Stress

Background:

  • Alkaline phosphatase is a crucial enzyme involved in various biological processes.
  • Mixed function oxidation systems can lead to enzyme inactivation.
  • Hydroxyl radicals are potent oxidants implicated in cellular damage.

Purpose of the Study:

  • To investigate the mechanism of alkaline phosphatase inactivation by mixed function oxidation systems.
  • To identify the specific reactive species responsible for oxidative damage.
  • To evaluate the protective effects of antioxidants against enzyme modification.

Main Methods:

  • Enzyme activity assays were performed on alkaline phosphatase.
  • Mixed function oxidation systems (Haber-Weiss cycle, Fenton-type reaction) were employed to generate hydroxyl radicals.

Related Experiment Videos

  • Hydroxyl radical scavengers, including uric acid and Vitamin E, were used.
  • Enzyme substrates, products, and metal cofactors were analyzed.

    • Main Results:

    • Alkaline phosphatase was inactivated by hydroxyl radicals generated through mixed function oxidation.
    • Evidence suggests a site-specific radical attack occurred at or near the enzyme's active center.
    • Uric acid demonstrated significant protective effects against alkaline phosphatase modification.
    • Vitamin E did not provide protection to the enzyme.

    Conclusions:

    • Hydroxyl radicals are key mediators in the oxidative inactivation of alkaline phosphatase.
    • The active site of alkaline phosphatase is particularly vulnerable to radical attack.
    • Uric acid is a potent scavenger of radicals that protects alkaline phosphatase from oxidative damage.