Experimental evidence for a two-step process in the aggregation of beta-lactoglobulin at pH 7

被引:83
作者
Aymard, P [1 ]
Gimel, JC [1 ]
Nicolai, T [1 ]
Durand, D [1 ]
机构
[1] UNIV MAINE,LAB CHIM & PHYSICOCHIM MACROMOL,CNRS URA 509,F-72017 LE MANS,FRANCE
关键词
globular protein; beta-lactoglobulin; aggregation; scattering techniques; size-exclusion chromatography;
D O I
10.1051/jcp/1996930987
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
A two-step mechanism for beta-lactoglobulin aggregation at pH7 has been reported in the literature. The first aggregation step is difficult to characterise, as small particles are formed with a strong tendency to further associate in bigger aggregates. Experimental evidence for a two-step aggregation process, using scattering techniques and size exclusion chromatography, is shown here. The effect of the ionic strength, the protein concentration and the heating temperature is discussed. The results show that the first step consists in the formation of small globular aggregates, whose size are only weakly, if at all, influenced by the parameters mentioned above.
引用
收藏
页码:987 / 997
页数:11
相关论文
共 15 条