Thermal stability of lysozyme and myoglobin in the presence of anionic surfactants

被引:28
作者
Blanco, Elena [1 ]
Ruso, J. M. [1 ]
Sabin, J. [1 ]
Prieto, G. [1 ]
Sarmiento, F. [1 ]
机构
[1] Univ Santiago de Compostela, Grp Biophys & Interfaces, Dept Appl Phys, Fac Phys, Santiago De Compostela 15782, Spain
关键词
lysozyme; myoglobin; thermal denaturation; thermodynamics; UV absorbance;
D O I
10.1007/s10973-006-7842-5
中图分类号
O414.1 [热力学];
学科分类号
摘要
The interactions of lysozyme and myoglobin with anionic surfactants (hydrogenated and fluorinated), at surfactant concentrations below the critical micelle concentration, in aqueous solution were studied using spectroscopic techniques. The temperature conformational transition of globular proteins by anionic surfactants was analysed as a function of denaturant concentration through absorbance measurements at 280 nm. Changes in absorbance of protein-surfactant system with temperature were used to determine the unfolding thermodynamics parameters, melting temperature, T-m, enthalpy, Delta H-m, entropy, Delta S-m and the heat capacity change, Delta C-p, between the native and denatured states.
引用
收藏
页码:211 / 215
页数:5
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