High dimensional structure of the antigen-binding site of anti-viomycin immunoglobulin analyzed by enzyme immunoassay.
Precise immunological recognition of anti-viomycin antiserum at detailed parts in the structure of viomycin was studied by cross reactivities of the antiserum to viomycin and its ten analogs using an enzyme immunoassay of viomycin. The antiserum clearly recognized all minor modifications in the sixteen membered ring of viomycin, indicating that the antiserum clearly recognizes the whole structure of the sixteen membered ring. Recognition of the antiserum on the beta-lysine terminus was also examined showing that the antiserum was also recognized on this part. Thus, the anti-viomycin antiserum was deduced to recognize the whole structure of viomycin, from which the deduction was made that the anti-viomycin antibodies in the antiserum must possess cavities fitting the whole structure of viomycin. The crystal dimensions of viomycin are 13 A in length, 8 A in width, and 7 A in depth. Thus, the high dimensional structure of the binding sites of the anti-viomycin antibodies was deduced to possess cavities of a similar size to that of viomycin.
D000818:Animals; D000941:Antigens / Q000032:analysis*; D001666:Binding Sites, Antibody; D003429:Cross Reactions; D007120:Immunochemistry; D007124:Immunoenzyme Techniques; D007136:Immunoglobulins / Q000032:analysis; D011817:Rabbits; D014756:Viomycin / Q000276:immunology*
D000941:Antigens; D007136:Immunoglobulins; D014756:Viomycin