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- W2007472212 abstract "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 °C. 6. The microcalorimetric measurements have been used to estimate enthalpy changes (ΔHd) on unfolding of trypsin; ΔHd 82 ± 5kJ·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." @default.
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- W2007472212 date "1977-03-01" @default.
- W2007472212 modified "2023-09-27" @default.
- W2007472212 title "A microcalorimetric study of the interaction between trysin and sodium n-dodecyl sulphate" @default.
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- W2007472212 doi "https://doi.org/10.1016/0005-2795(77)90047-2" @default.
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