Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid
| Autor: | R. W. Brown, J M Ring, Jock K. Findlay, David Robertson, Hearn Milton Thomas William, G S Cobon, R G Forage, B V McInerney, Morgan Francis Joseph, R P Gregson |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
chemistry.chemical_classification
Messenger RNA Multidisciplinary Base Sequence Sequence analysis Protein subunit Protein primary structure DNA Biology Molecular cloning Molecular biology Amino acid Molecular Weight Ovarian Follicle chemistry Complementary DNA Animals Cattle Female Inhibins Amino Acid Sequence Cloning Molecular Peptide sequence Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 83:3091-3095 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.83.10.3091 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|