Intermolecular Interactions in Solutions of Serum Albumin

被引：7
|
作者：
Polyanichko A.M. [1 ,2 ]
Mikhailov N.V. [1 ]
Romanov N.M. [1 ]
Baranova Y.G. [1 ]
Chikhirzhina E.V. [2 ]
机构：
[1] St. Petersburg State University, St. Petersburg
[2] Institute of Cytology, Russian Academy of Sciences, St. Petersburg
来源：
Cell and Tissue Biology | 2017年 / 11卷 / 1期
关键词：
analytical ultracentrifugation; dynamic light scattering; serum albumin;
D O I：
10.1134/S1990519X17010084
中图分类号：
学科分类号：
摘要：
The mechanisms of intermolecular protein complex formation were studied by the example of monomers, oligomers and aggregates of bovine serum albumin (BSA) depending on the protein concentration, pH and urea concentration. Using dynamic light scattering (DLS), analytical ultracentrifugation (AUC) and PAG electrophoresis we have shown the existence of dynamic equilibrium between monomers and aggregates in BSA solution. Decreasing pH of the solution (4.0–1.0) resulted in increasing sizes of the aggregates. In the solutions with low urea concentrations (below 2 M) the sizes of aggregates decreased, while higher urea concentrations (2–8 M) induced formation of larger aggregates due to the unfolding of the protein. © 2017, Pleiades Publishing, Ltd. All Right Reserved.
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页码：9 / 15
页数：6
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