| Autor: |
Leversha, L. J., Robertson, D. M., de Vos, F. L., Morgan, F. J., Hearn, M. T. W., Wettenhall, R. E. H., Findlay, J. K., Burger, H. G., de Kretser, D. M. |
| Zdroj: |
Journal of Endocrinology; May 1987, Vol. 113 Issue: 2 p213-221, 9p |
| Abstrakt: |
Two forms of inhibin with molecular weights of 65 000 and 30 000 (65 and 30 kD) were isolated from ovine follicular fluid using a combination of gel permeation chromatography, reversed-phase high-performance liquid chromatography and preparative polyacrylamide gel electrophoresis. The 65 kD form was partially purified approximately 315-fold whilst the 30 kD form was isolated as two isoforms (29 and 30 kD) of similar biological activity and in >95% purity (1210-fold purification and 4·2% recoveries). On reduction the 30 kD form resolved into four components of 36, 31, 20–21 and 16 kD of which the 20–21 and 16 kD components were similar to the corresponding inhibin subunits isolated from porcine and bovine follicular fluid. The 36 kD component was established as a non-reducible inhibin-like material, based on its binding to antiserum raised against bovine 58 kD inhibin. The nature of the remaining non-reducible 31 kD component is unknown. Two NH2-terminal amino acid sequences (first 13 amino acids) identified in purified 30 kD inhibin were identical to the corresponding subunit amino acid sequences of bovine 31 kD inhibin.J. Endocr.(1987) 113,213–221 |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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