Abstract
Both quantitative and qualitative estimations of the basidiomycete Grifola frondosa lectin binding to the specific and non-specific polyclonal rabbit antibodies were attempted. The lectin complexation with homological antibodies was shown to be characterized by greater binding constants as compared to non-homological antibodies. Therewith the values of changes in standard free energy ∆G 0 displaying a strength of both complexes were essentially the same. The data obtained testify to universality of biospecific reactions “antigen–antibody” and “lectin–carbohydrate” at a molecular level, and could give new insight into the phenomenon of these biospecific interactions. The actual specificity in the above bio-recognition processes could differ from the results of in vitro assays using lectins, and, therefore, should be interpreted carefully when concluding on the lectins behaviour in living systems.
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Acknowledgments
We thank our colleagues from the Institute of Biochemistry and Physiology of Plants and Microorganisms of the RAS: Prof. V.A. Bogatyrev for help in marking the lectin with colloidal gold; Prof. S.U. Shchegolev and Dr. E.E. Fedorov for valuable discussion.
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Stepanova, L.V., Burygin, G.L., Nikitina, V.E. et al. On the role of carbohydrate-protein highly selective interactions in the biological activity of glycoconjugates: Grifola frondosa (Fr.) S.F. Gray lectin binding to specific and non-specific antibodies. World J Microbiol Biotechnol 27, 1579–1585 (2011). https://doi.org/10.1007/s11274-010-0610-5
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DOI: https://doi.org/10.1007/s11274-010-0610-5