ÉTUDE DES EFFETS ÉLECTROSTATIQUES SUR LE MÉCANISME D'ACTION CATALYTIQUE DE LA PHOSPHATASE ALCALINE INTESTINALE DE VEAU
- 1 August 1965
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Chemistry
- Vol. 43 (8) , 2222-2235
- https://doi.org/10.1139/v65-300
Abstract
The influence of dioxane and ethanol on the rate of hydrolysis of p-nitrophenyl phosphate in the presence of an intestinal alcaline phosphatase can be interpreted as a dielectric constant effect, at high substrate concentration. The dielectric constant effect is a function of the pH of the medium and is maximum around pH 9.4 at 25 °C and pH 9.0 at 15 °C. An interpretation suggesting that the change in diameter of the enzyme molecule becoming an activated complex is minimum at a pH of maximum activity is proposed. The same model can take into account the influence of the ionic strength on the same reaction.This publication has 3 references indexed in Scilit:
- PHOSPHATASE ALCALINE INTESTINALE: CINÉTIQUE DE L'HYDROLYSE DU PHOSPHATE DE p-NITROPHÉNYLECanadian Journal of Chemistry, 1961
- INTRAMOLECULAR MODELS DEPICTING THE KINETIC IMPORTANCE OF „FIT” IN ENZYMATIC CATALYSISProceedings of the National Academy of Sciences, 1960
- The trypsin-catalyzed hydrolysis of benzoyl-l-arginine ethyl esterBiochimica et Biophysica Acta, 1960