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

FEBS Letters

Margaret, Daniels¹  Wallis, Michael¹ 

[1] Biochemistry Laboratory, School of Biological Sciences, University of Sussex, Falmer, Brighton, Sussex BN1 9QG, England

关键词: Human growth hormone;    Monoclonal antibody;    Plasmin digestion;    Radioimmunoassay;    Immunological epitope;    hGH;    human growth hormone;    McAb;    monoclonal antibody;    hPL;    human placental lactogen;   

DOI  :  10.1016/0014-5793(83)80455-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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, 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.

【 授权许可】

Unknown