| Autor: |
Robertson DM; Dept. of Anatomy, Monash University, Melbourne, Australia., Klein R, de Vos FL, McLachlan RI, Wettenhall RE, Hearn MT, Burger HG, de Kretser DM |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1987 Dec 16; Vol. 149 (2), pp. 744-9. |
| DOI: |
10.1016/0006-291x(87)90430-x |
| Abstrakt: |
Three proteins (31, 35 and 39 kDa) with inhibin-like activity have been isolated from bovine follicular fluid with identical NH2-terminal amino acid sequences. These polypeptides are distinct from inhibin, based on their different NH2-amino acid sequence, molecular masses, absence of a subunit structure, absence of inhibin immunoactivity and the failure of inhibin antiserum to neutralize their bioactivity in vitro. Their inhibin-like biological activities based on their ability to suppress FSH cell content by pituitary cells in culture are 5-10% of bovine 31 kDa inhibin. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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