Aggregation of β-lactoglobulin and influence of D2O

被引：35

作者：

Verheul, M ^{[1
]}

Roefs, SPFM ^{[1
]}

de Kruif, KG ^{[1
]}

机构：

[1] Netherlands Inst Dairy Res, NL-6710 BA Ede, Netherlands

来源：

FEBS LETTERS | 1998年 / 421卷 / 03期

关键词：

D2O; beta-lactoglobulin; protein stability; protein aggregation; light scattering; differential scanning calorimetry;

D O I：

10.1016/S0014-5793(97)01581-0

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 conformational stability of beta-lactoglobulin increases in D2O over that in H2O. This is concluded from an increase in peak temperature by about 3 degrees C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration on the heat-induced aggregation (reaction kinetics, DSC thermograms and aggregate growth) are similar in H2O and D2O. This indicates that the mechanism of heat-induced aggregation of beta-lactoglobulin is not significantly affected by replacement of H2O with D2O. (C) 1998 Federation of European Biochemical Societies.

引用

页码：273 / 276

页数：4

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