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

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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