Polyanichko A M, Mikhailov N V, Romanov N M, Baranova Yu G, Chikhirzhina E V
Tsitologiia. 2016;58(9):707-13.
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.
以牛血清白蛋白（BSA）的单体、寡聚体和聚集体为例，研究了分子间蛋白质复合物形成的机制，该机制取决于蛋白质浓度、pH值和尿素浓度。通过动态光散射（DLS）、分析超速离心（AUC）和聚丙烯酰胺凝胶电泳，我们发现BSA溶液中的单体和聚集体之间存在动态平衡。溶液pH值降低（4.0—1.0）会导致聚集体尺寸增大。在低尿素浓度（低于2 M）的溶液中，聚集体尺寸减小，而较高的尿素浓度会因蛋白质展开而诱导形成更大的聚集体。
