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 that there is 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 induced formation of larger aggregates due to the unfolding of the protein.

Translated title of the contributionINTERMOLECULAR INTERACTIONS IN THE SOLUTIONS OF SERUM ALBUMIN
Original languageRussian
Pages (from-to)707-713
Number of pages7
JournalЦитология
Volume58
Issue number9
StatePublished - 2016

    Research areas

  • Serum albumin, Analytical ultracentrifugation, DYNAMIC LIGHT SCATTERING

    Scopus subject areas

  • Pathology and Forensic Medicine
  • Histology

ID: 7588156