Immunogenicity of glucagon: determinants responsible for antibody binding and lymphocyte stimulation

Abstract

Bovine glucagon, a polypeptide of 29 amino acids, is immunogenic in rabbits and guinea pigs. The antigenic determinants of glucagon were investigated with isolated tryptic peptides of the hormone. Antibodies from virtually all of more than a dozen animals tested had specificity primarily for the aminoterminal heptadecapeptide. However, only intact glucagon and its carboxy-terminal dodecapeptide stimulated spleen or lymph node cells to synthesize DNA. It thus appears that glucagon was cleaved along functional lines into two parts, one of which contained the major antigenic determinant for serum antibody and the other of which was "recognized" by antigen-reactive cells.