title: 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.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D000939:Epitopes; D005341:Fibrinolysin / Q000494:pharmacology*; D013006:Growth Hormone / Q000276:immunology*; D006801:Humans; D010446:Peptide Fragments / Q000276:immunology*
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D000939:Epitopes; D010446:Peptide Fragments; D013006:Growth Hormone; D005341:Fibrinolysin