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Vol 34(2018) N 4 p. 62-66; DOI 10.21519/0234-2758-2018-34-4-62-66
E.A. Bormotova, T.V. Gupalova*

Purification of Immunoglobulin G by Affinity Chromatography using New Recombinant IgG-Binding Polypeptides as Ligands

Institute of Experimental Medicine, 197376, Saint Petersburg Russia

*tvgupalova@rambler.ru
Received - 16.04.2018; Accepted - 28.06.2018

References

Highly purified human and rabbit IgG preparations have been obtained by the method of affinity chromatography using two synthesized affinity sorbents as ligands that were obtained by the immobilization of an IgG-binding G4223 or G14223 recombinant polypeptide on a matrix (bromocyanogen-activated Sepharose 4B). IgG from rabbit serum contained specific antibodies to the Streptococcus group polysaccharides of A and B groups. Such IgG preparations make it possible to identify group-specific antigens of streptococci of these groups.

IgG purification, Sepharose 4В-G4223, Sepharose 4В-G14223, IgG-binding polypeptides G4223 and G14223, group streptococcal polysaccharides.



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