Binding specificity of monoclonal antibodies towards fragments of human growth hormone produced by plasmin digestion

Abstract

To help define the immunological epitopes on human growth hormone (hGH), interaction of fragments of the hormone with 7 monoclonal antibodies (McAbs) was studied. Plasmin-digested hGH, containing two peptides (hGH1−134 and hGH141−191) joined by a disulphide bond, bound to each McAb with affinity similar to that of intact hGH. The purified C-terminal fragment, hGH141−191, showed low affinity for each McAb. The N-terminal fragment, hGH1−134, bound with quite high affinity to 2 McAbs (EB1 and EB3) but not to the other 5. We conclude that residues 1−134 of hGH contain the epitope to which McAbs EB1 and EB3 bind