Epitope mapping by chemical modification of free and antibody-bound protein antigen.
A monoclonal antibody bound to a protein antigen slows the rate of chemical modification of amino acid residues located at the epitope. By comparing the degree of acetylation of 18 lysine and 7 threonine residues in free and antibody-bound horse cytochrome c, a discontiguous, conformational epitope was characterized on this protein antigen. The new approach is particularly suitable to probe discontiguous and conformational epitopes, which are difficult to analyze by other procedures.
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000936:Antigen-Antibody Complex; D003574:Cytochrome c Group / Q000276:immunology*; D000939:Epitopes / Q000276:immunology*; D006736:Horses; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D003574:Cytochrome c Group; D000939:Epitopes