Thermodynamics of the interaction of sodium-n-dodecyl sulphate with Aspergillus niger catalase in high ionic strength aqueous solutions.
The thermodynamic parameters for the interaction between sodium n-dodecyl sulphate (SDS) and Aspergillus niger catalase in aqueous solution at pH 3.2 and 6.4 have been measured by microcalorimetry and equilibrium dialysis over a range of ionic strength from 0.05 to 0.2 at 25 degrees C. Binding isotherms have been interpreted in terms of theoretical models (Hill equation and Wyman binding potential). The Gibbs energies of interaction become increasingly negative with increase in ionic strength and the entropies of interaction become increasingly positive. The ionic strength dependence of the Gibbs energies are much greater than predicted by the Debye-Hückel limiting law indicating a strongly ionic strength dependent hydrophobic contribution to the interactions.
Mosavi-Movahedi
A A
AA
Department of Biochemistry and Molecular Biology, University of Manchester, UK.
Jones
M M
MM
Pilcher
G
G
D001234:Aspergillus niger / Q000201:enzymology*; D002151:Calorimetry; D002374:Catalase / Q000378:metabolism*; D003956:Dialysis; D006863:Hydrogen-Ion Concentration; D012967:Sodium Dodecyl Sulfate / Q000378:metabolism*; D012996:Solutions; D013816:Thermodynamics
D012996:Solutions; D012967:Sodium Dodecyl Sulfate; D002374:Catalase