Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K
Both microcalorimetric determination of displacement adsorption enthalpies DeltaH and measurement of adsorbed amounts of guanidine - denatured lysozyme (Lys) refolding on the surface of hydrophobic interaction chromatography (HIC) packings at 308 K were carried out and compared with that at 298 K. S...
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| Veröffentlicht in: | Journal of thermal analysis and calorimetry 2006-09, Vol.85 (3), p.601-608 |
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| container_title | Journal of thermal analysis and calorimetry |
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| creator | GENG, X. P WU, Y. N WANG, B. H ZHANG, H. F GENG, X. D XING, J. W |
| description | Both microcalorimetric determination of displacement adsorption enthalpies DeltaH and measurement of adsorbed amounts of guanidine - denatured lysozyme (Lys) refolding on the surface of hydrophobic interaction chromatography (HIC) packings at 308 K were carried out and compared with that at 298 K. Study shows that both temperature and concentration of guanidine hydrochloride (GuHCl) affect the molecular mechanism of hydrophobic interaction of protein with adsorbent based on the analysis of dividing DeltaH values into three kinds of enthalpy fractions. The adsorption in higher concentrations of GuHCl ( > 1.3 mol L) at 308 K is an enthalpy-driving process, and the adsorption under other GuHCl concentrations is an entropy-driving process. The fact that the Lys denatured by 1.8 mol L GuHCl forms a relatively stable intermediate state under the studied conditions will not be changed by temperature. |
| doi_str_mv | 10.1007/s10973-006-7645-8 |
| format | Article |
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The adsorption in higher concentrations of GuHCl ( > 1.3 mol L) at 308 K is an enthalpy-driving process, and the adsorption under other GuHCl concentrations is an entropy-driving process. The fact that the Lys denatured by 1.8 mol L GuHCl forms a relatively stable intermediate state under the studied conditions will not be changed by temperature.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. 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| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology General aspects, investigation methods Proteins |
| title | Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K |
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