Intermolecular interactions in solutions of serum albumin
- Authors: Polyanichko A.M.1,2, Mikhailov N.V.1, Romanov N.M.1, Baranova Y.G.1, Chikhirzhina E.V.2
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Affiliations:
- St. Petersburg State University
- Institute of Cytology
- Issue: Vol 11, No 1 (2017)
- Pages: 9-15
- Section: Article
- URL: https://journals.rcsi.science/1990-519X/article/view/212235
- DOI: https://doi.org/10.1134/S1990519X17010084
- ID: 212235
Cite item
Abstract
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.
About the authors
A. M. Polyanichko
St. Petersburg State University; Institute of Cytology
Author for correspondence.
Email: a.polyanichko@spbu.ru
Russian Federation, St. Petersburg, 199034; St. Petersburg, 194064
N. V. Mikhailov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Russian Federation, St. Petersburg, 199034
N. M. Romanov
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Russian Federation, St. Petersburg, 199034
Yu. G. Baranova
St. Petersburg State University
Email: a.polyanichko@spbu.ru
Russian Federation, St. Petersburg, 199034
E. V. Chikhirzhina
Institute of Cytology
Email: a.polyanichko@spbu.ru
Russian Federation, St. Petersburg, 194064