Open AccessThermochemistry of Lysozyme‐Inhibitor Binding
Author(s) -
Bjurulf Carin,
Wadsö Ingemar,
Laynez José
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00259.x
Subject(s) - thermochemistry , lysozyme , glucosamine , chemistry , aqueous solution , calorimetry , muramidase , chromatography , thermodynamics , biochemistry , inorganic chemistry , physics
A microcalorimetric method has been used to study the binding of saccharide inhibitors to lysozyme in aqueous solution at pH 5 and 25°. Inhibitors studied were N ‐acetyl‐ d ‐glucosamine, di‐ N ‐acetyl‐ d ‐glucosamine and tri‐ N ‐acetyl‐ d ‐glucosamine. From the results of the calorimetric measurements Δ G°, Δ H° and Δ S° for the binding processes were calculated. Derived data have been compared with corresponding values obtained by various equilibrium measurements.