The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin

Biochem Biophys Res Commun. 1987 Dec 16;149(2):744-9. doi: 10.1016/0006-291x(87)90430-x.


Three proteins (31, 35 and 39 kDa) with inhibin-like activity have been isolated from bovine follicular fluid with identical NH2-terminal amino acid sequences. These polypeptides are distinct from inhibin, based on their different NH2-amino acid sequence, molecular masses, absence of a subunit structure, absence of inhibin immunoactivity and the failure of inhibin antiserum to neutralize their bioactivity in vitro. Their inhibin-like biological activities based on their ability to suppress FSH cell content by pituitary cells in culture are 5-10% of bovine 31 kDa inhibin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Female
  • Follicle Stimulating Hormone / antagonists & inhibitors*
  • Follicle Stimulating Hormone / metabolism
  • Inhibins / analysis
  • Inhibins / pharmacology*
  • Male
  • Molecular Weight
  • Ovarian Follicle / analysis*
  • Peptides / isolation & purification*
  • Peptides / pharmacology
  • Rats
  • Rats, Inbred Strains


  • Peptides
  • Inhibins
  • Follicle Stimulating Hormone