CALORIMETRIC STUDY OF COLD AND THERMAL DENATURATION OF BOVINE β-LACTOGLOBULIN B

被引：1
|
作者：
Bang Ning WANG and Fu TAN Institute of Chemistry
机构：
来源：
Chinese Chemical Letters | 1993年 / 11期
基金：
中国国家自然科学基金;
关键词：
In; LACTOGLOBULIN B; CALORIMETRIC STUDY OF COLD AND THERMAL DENATURATION OF BOVINE;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The denaturational behaviour of bovine β-lactoglobulin B has been studied in solutions containing guanidine hydrochloride by differential scanning calorimetry. The experiments have shown that complete peaks of cold denaturation can be recorded also in high concentration of protein solutions. The cold denaturation and the renaturation of the protein are reproducible, but the thermal denaturation is irreversible. The activation energy of thermal denaturation calculated is about 285 kJ/mol.
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页码：971 / 974
页数：4
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