Early conformational changes and activity modulation induced by guanidinium chloride on intestinal alkaline phosphatase

Risultato della ricerca: Contributo in rivistaArticolo in rivista

11 Citazioni (Scopus)

Abstract

Moderate concentrations of guanidinium chloride induce both instantaneous and time-dependent modifications of the catalytic and optical properties of intestinal alkaline phosphatase, which undergoes consecutive conformational transitions at about 0.05 M, 0.25 M and 1.0 M denaturant. A paradoxical activation is observed up to 1.0 M-guanidine, with a maximum at 0.25 M- and a mid-point around 0.5 M-guanidine. Difference absorbance and fluorescence spectra imply a change in the state of ionization of the protein residues, with variation in molecular size suggested by light-scattering. Random-coil formation is indicated by a lower fluorescence yield, a more polar environment of the aromatic residues and another separate tryptophan emission. Iodide quenching confirms the alterations of conformation. Deprotonation favours the loss of the intramolecular constraints and the enhancement of the structure disruption by guanidine.
Lingua originaleEnglish
pagine (da-a)551-556
Numero di pagine6
RivistaBiochemical Journal
Volume248
Stato di pubblicazionePubblicato - 1987

Keywords

  • Alkaline Phosphatase
  • Animals
  • Cattle
  • Enzyme Activation
  • Guanidine
  • Guanidines
  • Hydrogen-Ion Concentration
  • Intestines
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Spectrophotometry

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