Intermolecular interactions in solutions of serum albumin
- Autores: Polyanichko A.1,2, Mikhailov N.1, Romanov N.1, Baranova Y.1, Chikhirzhina E.2
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Afiliações:
- St. Petersburg State University
- Institute of Cytology
- Edição: Volume 11, Nº 1 (2017)
- Páginas: 9-15
- Seção: Article
- URL: https://journals.rcsi.science/1990-519X/article/view/212235
- DOI: https://doi.org/10.1134/S1990519X17010084
- ID: 212235
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Resumo
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.
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Sobre autores
A. Polyanichko
St. Petersburg State University; Institute of Cytology
Autor responsável pela correspondência
Email: a.polyanichko@spbu.ru
Rússia, St. Petersburg, 199034; St. Petersburg, 194064
N. Mikhailov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Rússia, St. Petersburg, 199034
N. Romanov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Rússia, St. Petersburg, 199034
Yu. Baranova
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Rússia, St. Petersburg, 199034
E. Chikhirzhina
Institute of Cytology
Email: a.polyanichko@spbu.ru
Rússia, St. Petersburg, 194064