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Probing Human Follicle Stimulating Hormone with Monoclonal Antibodies and Synthetic Peptides

  • P. Berger
  • S. Dirnhofer
  • R. Klieber
  • R. Frank
  • G. Wick
Part of the Serono Symposia USA book series (SERONOSYMP)

Abstract

The antigenic topography of the closely related molecules human follicle stimulating hormone (hFSH), human chorionic gonadotropin (hCG), and human luteinizing hormone (hLH) was previously elucidated (1–3) with extensively characterized monoclonal antibodies (MCA) against hFSH (1), hCG (4), bovine LH (bLH) (5), and the free subunits of hCG (6). The structural similarities of the glycoprotein hormones are well established (7); they all consist of 2 subunits designated α and β. In humans, the former is encoded by a single gene and is thus identical for each member of this family, whereas the latter is different from hormone to hormone and is therefore known to mediate biological specificity. Schematic epitope maps were taken as a basis for the alignment of antigenic and receptor interaction domains. The aim of the present study was to localize epitopes on hFSH at the amino acid sequence level with synthetic peptides and to describe the biological role they may play. We focused on the question of whether and, if so, in which way MCA and synthetic peptides interfere with hFSH receptor (hFSH-R) interaction.

Keywords

Human Chorionic Gonadotropin Glycoprotein Hormone Amino Acid Sequence Level Human Follicle Entire Amino Acid Sequence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Berger P, Panmoung W, Khaschabi D, Mayregger B, Wick G. Antigenic features of human follicle stimulating hormone delineated by monoclonal antibodies and construction of an immunoradiometric assay (IRMA). Endocrinology 1988; 123: 2351.Google Scholar
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Copyright information

© Springer-Verlag New York, Inc. 1992

Authors and Affiliations

  • P. Berger
  • S. Dirnhofer
  • R. Klieber
  • R. Frank
  • G. Wick

There are no affiliations available

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