par Schlusselberg, Jean 
;Paredes, Sergio
Référence BBA - Protein Structure, 405, 1, page (89-98)
Publication Publié, 1975-09
;Paredes, Sergio Référence BBA - Protein Structure, 405, 1, page (89-98)
Publication Publié, 1975-09
Article révisé par les pairs
| Résumé : | Activity coefficients of alcohols in Raoult's reference system have been calculated. Using data from papers dealing with transition temperatures in the presence of n-alcohols, lipase deactivation and competitive inhibition by n-alcohols of pepsin and α-chymotrypsin, it is shown that the conversion of concentrations into activities (using Pierotti's equation) profoundly affects the original data. Within experimental error, if inhibition constants by alcohols keep the same value, lipase deactivation becomes independent of the length of the alcohol chain, and except for butanol, transition temperature is no longer dependent on the number of methylene groups. Interpretations which take into account the thermodynamic reference system and final environment are related to the fact that alcohol molecules bind to some inner parts of the proteins. © 1975. |
