Intermolecular interactions in solutions of serum albumin
- 作者: Polyanichko A.1,2, Mikhailov N.1, Romanov N.1, Baranova Y.1, Chikhirzhina E.2
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隶属关系:
- St. Petersburg State University
- Institute of Cytology
- 期: 卷 11, 编号 1 (2017)
- 页面: 9-15
- 栏目: Article
- URL: https://journals.rcsi.science/1990-519X/article/view/212235
- DOI: https://doi.org/10.1134/S1990519X17010084
- ID: 212235
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详细
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.
作者简介
A. Polyanichko
St. Petersburg State University; Institute of Cytology
编辑信件的主要联系方式.
Email: a.polyanichko@spbu.ru
俄罗斯联邦, St. Petersburg, 199034; St. Petersburg, 194064
N. Mikhailov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
俄罗斯联邦, St. Petersburg, 199034
N. Romanov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
俄罗斯联邦, St. Petersburg, 199034
Yu. Baranova
St. Petersburg State University
Email: a.polyanichko@spbu.ru
俄罗斯联邦, St. Petersburg, 199034
E. Chikhirzhina
Institute of Cytology
Email: a.polyanichko@spbu.ru
俄罗斯联邦, St. Petersburg, 194064