Abstract

Very low amounts of ascorbic acid modify alkaline phosphatase fluorescence, absorption and enzymatic activity. A strong quenching of enzyme, tryptophan and tyrosine emission together with evident alterations of the protein absorption characteristics are observed. The catalytic activity inhibition probably reflects a perturbation of the active site environment due to the interaction of ascorbic acid with enzyme aminoacyl residues.
Lingua originaleEnglish
pagine (da-a)231-238
Numero di pagine8
RivistaItalian Journal of Biochemistry
Volume32
Stato di pubblicazionePubblicato - 1983

Keywords

  • Alkaline Phosphatase
  • Animals
  • Ascorbic Acid
  • Cattle
  • Kidney
  • Spectrometry, Fluorescence

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