Thermal Study of Lysozyme Binding with β-Cyclodextrin

Abstract:

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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.

Info:

Periodical:

Edited by:

Wu Fan

Pages:

1966-1969

DOI:

10.4028/www.scientific.net/AMM.110-116.1966

Citation:

G. R. Behbehani and L. Barzegar, "Thermal Study of Lysozyme Binding with β-Cyclodextrin", Applied Mechanics and Materials, Vols. 110-116, pp. 1966-1969, 2012

Online since:

October 2011

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$35.00

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