A microacalorimetric study of the interaction between trypsin and sodium n-dodecyl sulphate.
1. The binding of sodium n-dodecyl sulphate to trypsin and reduced trypsin has been measured by equilibrium dialysis at pH 3.5 and 5.5. 2. At pH 3.5 trypsin specifically binds surfactant at low concentration, at higher concentrations co-operative binding occurs. 3. Reduction of trypsin destroys the specific binding sites at pH 3.5. 4. At pH 5.5 both trypsin and reduced trypsin show only co-operative binding. 5. The interaction of sodium n-dodecyl sulphate with trypsin, reduced, inhibited, and thermally denatured trypsins has been studied by microcalorimetry at 25 degrees C. 6. The microcalorimetric measurements have been used to estimate enthalpy changes (deltaHd) on unfolding of trypsin; deltaHd = 82 +/- 5 kJ-mol-1 at pH 3.5 and 128 +/- 5 kJ-mol-1 at pH 5.5. 7. The unfolding of trypsin follows a different thermochemical pathway to that of reduced trypsin.
D001665:Binding Sites; D002151:Calorimetry; D003956:Dialysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding; D012967:Sodium Dodecyl Sulfate; D013816:Thermodynamics; D014357:Trypsin
D012967:Sodium Dodecyl Sulfate; D014357:Trypsin