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  • Author or Editor: X. P. Geng x
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Summary  

Calorimetric determination of the total enthalpy changes (ΔH i) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobic interaction chromatography packings was carried out at 250.001C. The measured ΔH iin the circumstances should include the changes in the three fractions: adsorption, dehydration and molecular conformation. It was found that when the unfolded Lys molecules are adsorbed and refold on the surface, entropy-driving caused by the dehydration of Lys mainly dominates the foregoing process. The refolding enthalpies of Lys, ΔΔH iwere found to be 10~100 folds higher than that measured in usual solutions.</o:p>

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