Thermochemistry of Lysozyme‐Inhibitor Binding
- 1 November 1972
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 31 (1) , 95-102
- https://doi.org/10.1111/j.1432-1033.1972.tb02505.x
Abstract
The binding of saccharide inhibitors to lysozyme has been studied using a microcalorimetric method. Measurements have been performed with N‐acetyl‐d‐glucosamine (pH 5 and 25 and 40°C), tri[N‐acetyl‐d‐glucosamine] (pH 2, 5 and 7.6 at 25°C and pH 5 at 40°C) and with tetra‐[N‐acetyl‐d‐glucosamine] (pH 2, 5 and 7.6 at 25°C). From the results of the calorimetric measurements values for ΔG0, ΔH0, ΔS0, and ΔCp0 were derived for the binding processes.In addition to the saccharide‐binding reactions, some model experiments were performed.Keywords
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