Interaction between lysozyme and n-alkyl sulphates in aqueous solution
Abstract
The enthalpy changes on interaction of a series of sodium n-alkyl sulphates with lysozyme have been measured by microcalorimetry at 25°C in aqueous solution at pH 3.2 and 9.0. The enthalpy of interaction increases with increase in alkyl chain length and decrease in pH. Sodium n-decyl and n-dodecyl sulphates initiate a conformation change in lysozyme which makes an endothermic contribution to the overall enthalpy of interaction at high binding levels. Measurements of the binding isotherms and enthalpies of interactions of sodium n-dodecyl sulphate with derivatives of lysozyme in which the cationic residues lysyl, arginyl and histidyl have been chemically modified lead to the view that ionic groups are largely responsible for the initial exothermic interaction of the surfactant with the protein.
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