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Refolding of Lysozyme Upon Interaction with ?-Cyclodextrin
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نویسنده
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Rezaei Behbehani G. ,Taherkhani A. ,Barzegar L. ,Saboury A.A. ,Divsalar A.
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منبع
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journal of sciences islamic republic of iran - 2011 - دوره : 22 - شماره : 2 - صفحه:117 -120
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چکیده
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Effects of β-cyclodextrin, βcd, on refolding of lysozyme was investigated at ph 12 employing isothermal titration calorimetry (itc) at 300k in 30mm tris buffer solution. βcd was employed as an anti-aggregation agent and the heats obtained for lysozyme+βcd interactions are reported and analyzed in terms of the extended solvation model. it was indicated that there are two sets of identical and non-cooperative sites for βcd. enthalpic force in the first binding sites is more important than entropic one, indicating that electrostatic interaction plays an important role in the interaction of lysozyme with βcd. the interaction in the second binding sites is stronger and both enthalpy and entropy driven but hydrophobic interaction has more important than electrostatic force. these results suggest that the effects of βcd on lysozyme refolding are attributed to its ability to suppress aggregation of the protein
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کلیدواژه
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Lysozyme; Isothermal titration calorimetry; β-Cyclodextrin; Binding parameters
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آدرس
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islamic azad university, Faculty of Science, Chemistry Department, ایران, islamic azad university, Young Researchers Club, ایران. islamic azad university, Department of Physics, ایران, university of tehran, Institute of Biochemistry and Biophysics, ایران, university of tehran, Institute of Biochemistry and Biophysic, ایران, kharazmi university (university of tarbiat moallem), Department of Biological Sciences, ایران. university of tehran, Institute of Biochemistry and Biophysics, ایران
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Authors
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