HEAT AND COLD DENATURATION OF BETA-LACTOGLOBULIN-B

被引：40
作者：
AZUAGA, AI
GALISTEO, ML
MAYORGA, OL
CORTIJO, M
MATEO, PL
机构：
[1] UNIV GRANADA,FAC CIENCIAS,DEPT QUIM FIS,E-18071 GRANADA,SPAIN
[2] UNIV COMPLUTENSE MADRID,FAC FARM,DEPT QUIM FIS 2,E-28039 MADRID,SPAIN
[3] UNIV GRANADA,INST BIOTECHNOL,E-18071 GRANADA,SPAIN
来源：
FEBS LETTERS | 1992年 / 309卷 / 03期
关键词：
BETA-LACTOGLOBULIN-B; THERMAL STABILITY; COLD DENATURATION; GUANIDINE HYDROCHLORIDE; SCANNING CALORIMETRY; CIRCULAR DICHROISM;
D O I：
10.1016/0014-5793(92)80784-E
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The thermal denaturation of bovine beta-lactoglobulin B was investigated by high-sensitivity differential scanning microcalorimetry between pH 1.5 and 3.0 in 20 mM phosphate buffer. The process was found to be a reversible, two-state transition. Progressive addition of guanidine hydrochloride at pH 3.0 leads to the appearance of a low-temperature calorimetric endotherm, corresponding to the cold renaturation of the protein. Circular dichroism experiments have confirmed the low and high temperature denaturation processes, and have shown some structural differences between both denatured states of beta-lactoglobulin B.
引用
收藏
页码：258 / 260
页数：3
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