A MODEL FOR THE DENATURATION AND AGGREGATION OF BETA-LACTOGLOBULIN

被引:356
作者
ROEFS, SPFM
DEKRUIF, KG
机构
[1] Netherlands Institute for Dairy Research (Nizo), Ede
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 226卷 / 03期
关键词
D O I
10.1111/j.1432-1033.1994.00883.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
A quantitatively correct kinetic model for the temperature-induced denaturation and aggregation of beta-lactoglobulin is presented. The model recognizes an initiation, a propagation and a termination step by analogy with polymer radical chemistry. The decrease in native beta-lactoglobulin is predicted to follow order 3/2, in agreement with experimental results. The size of the protein polymer particles is predicted to be proportional to the square root of the initial beta-lactoglobulin concentration. The scattered light intensity is proportional to the product of concentration and size of the protein polymer particles. The initial increase in scattering intensity of the particles therefore scales with the initial squared beta-lactoglobulin concentration. The influence of other reaction conditions, e.g. ionic strength and pH, can be incorporated via the reaction constants of the reaction kinetic pathway.
引用
收藏
页码:883 / 889
页数:7
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