Mixed function oxidation and enzymes: kinetic and structural properties of an oxidatively modified alkaline phosphatase

Alvaro Mordente, Elisabetta Meucci, Ge Martorana, Ga Miggiano, Sa Santini, A. Castelli

Risultato della ricerca: Contributo in rivistaArticolo in rivista

7 Citazioni (Scopus)

Abstract

No major structural alteration of alkaline phosphatase can be observed in the early stages of enzyme oxidative inactivation by the ascorbate model system. Fluorescence changes of protein-bound 8-anilino-1-naphthalenesulfonic acid suggest, however, that localized modifications take place. Oxidized alkaline phosphatase displays less catalytic efficiency (decrease of Vmax), while retaining the other kinetic properties, including the same affinity for substrates and inhibitors and the same activation energy of the native enzyme. Typical features of the modified protein are a decreased thermal stability and a biphasic heat inactivation profile, which make the oxidized form quite similar to aged enzymes. The lower response to Mg2+ activation indicates that the magnesium binding sites of alkaline phosphatase are probably the targets of the ascorbate system oxidative modifications.
Lingua originaleEnglish
pagine (da-a)502-509
Numero di pagine8
RivistaArchives of Biochemistry and Biophysics
Volume264
Stato di pubblicazionePubblicato - 1988

Keywords

  • Alkaline Phosphatase
  • Anilino Naphthalenesulfonates
  • Animals
  • Catalysis
  • Cattle
  • Chemical Phenomena
  • Chemistry
  • Chromatography, High Pressure Liquid
  • Drug Stability
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation
  • Fluorescent Dyes
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Kinetics
  • Magnesium
  • Mixed Function Oxygenases
  • Oxidation-Reduction
  • Spectrometry, Fluorescence
  • Spectrophotometry
  • Structure-Activity Relationship

Fingerprint Entra nei temi di ricerca di 'Mixed function oxidation and enzymes: kinetic and structural properties of an oxidatively modified alkaline phosphatase'. Insieme formano una fingerprint unica.

Cita questo