Abstract

Two monoclonal antibodies recognizing distinct epitopes the outer boundaries of which are separated by only three amino acid residues, a maximum of 10A, were demonstrated to bind simultaneously to a short synthetic peptide. The affinity of binding of the two monoclonal antibodies and of Fab' fragments derived from them was determined. The stoichiometry of the interaction was analysed by velocity sedimentation and by gel permeation chromatography experiments. The results indicate that the immune complexes formed are composed of two antibody molecules in association with one or two peptide molecules.