Thermal stability of bovine serum albumin DSC study

被引：152

作者：

Michnik, A ^{[1
]}

机构：

[1] Univ Silesia, Inst Phys, Dept Med Phys, PL-40007 Katowice, Poland

来源：

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY | 2003年 / 71卷 / 02期

关键词：

albumin domains; bovine serum albumin; DSC; thermal stability; unfolding;

D O I：

10.1023/A:1022851809481

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

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 69degreesC with enthalpy change about 1000 kJ mol(-1). Defated albumin melts in two different temperature ranges: near 56 and 69degreesC with enthalpy changes about 300 and 200 kJ mol(-1) 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.

引用

页码：509 / 519

页数：11

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