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

Robert G. Forage, Jennifer M. Ring, Richard W. Brown, Bernard V. McInerney, Gary S. Cobon, Richard P. Gregson, David M. Robertson, Francis J. Morgan, Milton T. W. Hearn, Jock K. Findlay, Richard E. H. Wettenhall, Henry G. Burger, David M. de Kretser

Research output: Contribution to journalArticlepeer-review

250 Citations (Scopus)

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 OrkDa (A(C)) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.

Original languageEnglish
Pages (from-to)3091-3095
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number10
DOIs
Publication statusPublished - May 1986
Externally publishedYes

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