THERMAL STABILITY OF BOVINE SERUM ALBUMIN DSC study
نویسنده
چکیده
A calorimetric study of thermal denaturation of bovine serum albumin in aqueous solutions has shown essential differences in stability of fatty acid containing and defatted albumin. The first one shows a single endotherm peak in DSC curve near 69°C with enthalpy change about 1000 kJ mol. Defated albumin melts in two different temperature ranges: near 56 and 69°C with enthalpy changes about 300 and 200 kJ mol respectively. Deconvolution analysis shows that the single endotherm is well approximated as the sum of three independent two-state transitions. Two transitions of bimodal DSC curve for defatted albumin are not of a two-state type. This molecule melts probably as two structurally independent parts.
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