The presented work is devoted to the study of the chaperone activity of the recombinant protein Skp (rSkp) Yersinia pseudotuberculosis using dynamic light scattering and enzyme-linked immunosorbent assay. Commercial samples of rabbit polyclonal IgG antibodies and mouse monoclonal immunoglobulins, IgG1 isotype, were used as substrate proteins. It was found that rSkp is able to slow down the processes of self-association and aggregation of immunoglobulins, while maintaining their antigen-binding ability. For antibodies of each animal species, the chaperonic properties of the protein are manifested individually. The chaperone activity of rSkp significantly depends on the pH value of the medium in which the antibodies are located.
chaperone Skp, Yersinia pseudotuberculosis, immunoglobulin G, antibodies, aggregation
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