The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D005260:Female; D005640:Follicle Stimulating Hormone / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007265:Inhibins / Q000032:analysis / Q000494:pharmacology*; D008297:Male; D008970:Molecular Weight; D006080:Ovarian Follicle / Q000032:analysis*; D010455:Peptides / Q000302:isolation & purification* / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D010455:Peptides; D007265:Inhibins; D005640:Follicle Stimulating Hormone