Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid.
Proceedings of the National Academy of Sciences1986Vol. 83(10), pp. 3091–3095
Citations Over TimeTop 1% of 1986 papers
R G Forage, Jennifer M. Ring, R. W. Brown, Bernard V. McInerney, Gary S. Cobon, Richard P. Gregson, D.M. Robertson, Francis J. Morgan, Milton T. W. Hearn, Jock K. Findlay
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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