[Ligand-induced structuring of polyreactive immunoglobulins].
The influence of several hydrophobic compounds with different structures on the binding of native and chaotropically modified bovine immunoglobulins to native and denatured nonspecific protein immobilized on the surface is researched. It is shown that the character of binding depends on the amount and mutual location of hydrophobic nuclei in the effectors structure. The authors observed moderate suppression of binding or absence of the expressed effect while using one-nucleus effector. The influence of compounds with two distanced benzene nuclei differs qualitatively from the influence of the compound with two condensate ones, described earlier: it was observed that the stimulation level of the binding depends on structural-functional condition of immunoglobulin and immobilized protein. In case of the effector with three spaced hydrophobic nuclei the stimulating effect is much more expressed (3-4 times higher). The concentration dependence of the ligand-induced effects is demonstrated. It is supposed, that stimulative influence of effectors with spaced hydrophobic nuclei is caused by two different processes. The first one is the formation of highly binding center as the result of ligand-induced structuring of immunoglobulins. The other one is the competition for the center formed between dissolved polynuclear effector and ligand groups of aminoacids hydrophobic residues statistically formed on the surface of immobilized protein.
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Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv.
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D000818:Animals; D000941:Antigens / Q000276:immunology; D001666:Binding Sites, Antibody; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D006736:Horses; D057927:Hydrophobic and Hydrophilic Interactions; D007136:Immunoglobulins / Q000737:chemistry* / Q000276:immunology*; D008024:Ligands; D009211:Myoglobin / Q000276:immunology; D011487:Protein Conformation
D000941:Antigens; D007136:Immunoglobulins; D008024:Ligands; D009211:Myoglobin