Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid.

Authors:
  • RFR G Forage
    R G Forage
  • JRJ M Ring
    J M Ring
  • RBR W Brown
    R W Brown
  • GCG S Cobon
    G S Cobon
  • RGR P Gregson
    R P Gregson
  • DRD M Robertson
    D M Robertson
  • FMF J Morgan
    F J Morgan
  • MHM T Hearn
    M T Hearn
  • JFJ K Findlay
    J K Findlay
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Abstract
The primary amino acid structures of the 43-kDa (A) and 15-kDa (B) subunits of the 58-kDa form of the hormone inhibin have been elucidated by cloning and analysis of cDNA species derived from bovine granulosa cell mRNA. The A subunit (Mr = 32,298) is a protein of 300 amino acids with two potential N-glycosylation sites and two potential proteolytic processing sites and has a pre-pro region of 60 amino acids. The mature B subunit (Mr = 12,977) is a protein of 116 amino acids synthesized from a separate mRNA. These data establish that a 31-kDa form of inhibin also isolated from bovine follicular fluid, with subunits of 20 kDa (Ac) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.

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