Abstract
Three proteins (31, 35 and 39kDa) with inhibin-like activity have been isolated from bovine follicular fluid with identical NH 2-terminal amino acid sequences. These polypeptides are distinct from inhibin, based on their different NH 2-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 31kDa inhibin.
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