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Metal Substitution and Fluorescence Modifications in Ascorbate-Alkaline Phosphatase Interaction

  • G. E. Martorana
  • E. Meucci
  • G. A. D. Miggiano
  • A. Mordente
  • S. A. Santini
  • A. Castelli
Conference paper

Abstract

Alkaline phosphatase (EC 3.1.3.1), a zinc metallo-enzyme, is irreversibly inhibited by ascorbate, probably through a modification of active site environment (Martorana et al., 1986; Miggiano et al., 1984). A metal substituted form was prepared from bovine kidney alkaline phosphatase purchased from Calbiochem (La Jolla, CA, U.S.A.) and further purified as described (Martorana et al., 1986). Cobalt can replace zinc yielding a partially active phosphohydrolase, which lacks phosphotransferase activity (Ensinger et al., 1978) and presents a relevant visible absorption (Simpson and Vallee, 1968).

Keywords

Zinc Chloride Charge Transfer Mechanism Free Tryptophan Difference Absorption Spectrum Cobalt Sulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • G. E. Martorana
    • 1
  • E. Meucci
    • 1
  • G. A. D. Miggiano
    • 1
  • A. Mordente
    • 1
  • S. A. Santini
    • 1
  • A. Castelli
    • 1
  1. 1.Institute of Biological ChemistryCatholic UniversityRomeItaly

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