Multiple antigenic sites on an eicosapeptide. I. Precipitin studies in the goat.

Purified peptide 105-124, an antigenic determinant from the carboxy terminus ribonuclease, was found to form an immune precipitate with antibody to that region prepared by affinity chromatography from goat hyperimmune antiserum to reduced carboxymethylated ribonuclease (CM-RNase). Cm-rnase also gave an immune precipitate with the antibody. Purified antibody to another region of similar size (40-61) did not form a precipitate with CM-RNase but did co-precipitate in the presence of antibody to peptide 105-124 and CM-RNase. The precipitin reaction between antibody to peptide 105-124 and CM-RNase was inhibited by two synthetic derivatives, peptides 118-124 and ala114-RNase 114-124. Stoichiometry of the precipitin reactions of antibody to 105-124 with CM-RNase or peptide 105-124 suggested an antigen valency of three or more. Consistent with this both peptides 105-124 and ala114-RNase 114-124 elicited immediate cutaneous reactions but 118-124 did not. These findings suggest that the eicosapeptide 105-124 is multivalent since at least three antibodies can react simultaneously with it.