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

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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@article{Forage1986CloningAS, title={Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid.}, author={R G Forage and Jenny Ring and Roger W . Brown and Bernie V McInerney and Gary S. Cobon and R. P. Gregson and David M. Robertson and Fraser J. Morgan and Milton T. W. Hearn and Jock K. Findlay}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={1986}, volume={83 10}, pages={3091-5} }