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Binding specificity of monoclonal antibodies towards fragments of human growth hormone produced by plasmin digestion
Author(s) -
Wallis Michael,
Margaret Daniels
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80455-4
Subject(s) - monoclonal antibody , epitope , plasmin , chemistry , antibody , microbiology and biotechnology , biochemistry , human growth hormone , growth hormone , hormone , biology , enzyme , immunology
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 (hGH 1−134 and hGH 141−191 ) joined by a disulphide bond, bound to each McAb with affinity similar to that of intact hGH. The purified C‐terminal fragment, hGH 141−191 , showed low affinity for each McAb. The N‐terminal fragment, hGH 1−134 , 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.