Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 May;83(10):3091–3095. doi: 10.1073/pnas.83.10.3091

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

R G Forage, J M Ring, R W Brown, B V McInerney, G S Cobon, R P Gregson, D M Robertson, F J Morgan, M T Hearn, J K Findlay, et al.
PMCID: PMC323458  PMID: 3458167

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.

Full text

PDF
3091

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beksac M. S., Khan S. A., Eliasson R., Skakkebaek N. E., Sheth A. R., Diczfalusy E. Evidence for the prostatic origin of immunoreactive inhibin-like material in human seminal plasma. Int J Androl. 1984 Oct;7(5):389–397. doi: 10.1111/j.1365-2605.1984.tb00796.x. [DOI] [PubMed] [Google Scholar]
  3. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  4. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  6. Hanahan D., Meselson M. Plasmid screening at high colony density. Gene. 1980 Jun;10(1):63–67. doi: 10.1016/0378-1119(80)90144-4. [DOI] [PubMed] [Google Scholar]
  7. Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol. 1983 Jun 5;166(4):557–580. doi: 10.1016/s0022-2836(83)80284-8. [DOI] [PubMed] [Google Scholar]
  8. Hunkapiller M. W., Lujan E., Ostrander F., Hood L. E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 1983;91:227–236. doi: 10.1016/s0076-6879(83)91019-4. [DOI] [PubMed] [Google Scholar]
  9. Jacobs K., Shoemaker C., Rudersdorf R., Neill S. D., Kaufman R. J., Mufson A., Seehra J., Jones S. S., Hewick R., Fritsch E. F. Isolation and characterization of genomic and cDNA clones of human erythropoietin. 1985 Feb 28-Mar 6Nature. 313(6005):806–810. doi: 10.1038/313806a0. [DOI] [PubMed] [Google Scholar]
  10. Johansson J., Sheth A., Cederlund E., Jörnvall H. Analysis of an inhibin preparation reveals apparent identity between a peptide with inhibin-like activity and a sperm-coating antigen. FEBS Lett. 1984 Oct 15;176(1):21–26. doi: 10.1016/0014-5793(84)80904-7. [DOI] [PubMed] [Google Scholar]
  11. Li C. H., Hammonds R. G., Jr, Ramasharma K., Chung D. Human seminal alpha inhibins: isolation, characterization, and structure. Proc Natl Acad Sci U S A. 1985 Jun;82(12):4041–4044. doi: 10.1073/pnas.82.12.4041. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lilja H., Jeppsson J. O. Amino acid sequence of the predominant basic protein in human seminal plasma. FEBS Lett. 1985 Mar 11;182(1):181–184. doi: 10.1016/0014-5793(85)81179-0. [DOI] [PubMed] [Google Scholar]
  13. Ling N., Ying S. Y., Ueno N., Esch F., Denoroy L., Guillemin R. Isolation and partial characterization of a Mr 32,000 protein with inhibin activity from porcine follicular fluid. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7217–7221. doi: 10.1073/pnas.82.21.7217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mason A. J., Hayflick J. S., Ling N., Esch F., Ueno N., Ying S. Y., Guillemin R., Niall H., Seeburg P. H. Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-beta. Nature. 1985 Dec 19;318(6047):659–663. doi: 10.1038/318659a0. [DOI] [PubMed] [Google Scholar]
  15. McCullagh D. R. DUAL ENDOCRINE ACTIVITY OF THE TESTES. Science. 1932 Jul 1;76(1957):19–20. doi: 10.1126/science.76.1957.19. [DOI] [PubMed] [Google Scholar]
  16. Miyamoto K., Hasegawa Y., Fukuda M., Nomura M., Igarashi M., Kangawa K., Matsuo H. Isolation of porcine follicular fluid inhibin of 32K daltons. Biochem Biophys Res Commun. 1985 Jun 14;129(2):396–403. doi: 10.1016/0006-291x(85)90164-0. [DOI] [PubMed] [Google Scholar]
  17. Murray N. E., Brammar W. J., Murray K. Lambdoid phages that simplify the recovery of in vitro recombinants. Mol Gen Genet. 1977 Jan 7;150(1):53–61. doi: 10.1007/BF02425325. [DOI] [PubMed] [Google Scholar]
  18. Nevins J. R. The pathway of eukaryotic mRNA formation. Annu Rev Biochem. 1983;52:441–466. doi: 10.1146/annurev.bi.52.070183.002301. [DOI] [PubMed] [Google Scholar]
  19. Peacock S. L., McIver C. M., Monahan J. J. Transformation of E. coli using homopolymer-linked plasmid chimeras. Biochim Biophys Acta. 1981 Sep 28;655(2):243–250. doi: 10.1016/0005-2787(81)90014-9. [DOI] [PubMed] [Google Scholar]
  20. Robertson D. M., Foulds L. M., Leversha L., Morgan F. J., Hearn M. T., Burger H. G., Wettenhall R. E., de Kretser D. M. Isolation of inhibin from bovine follicular fluid. Biochem Biophys Res Commun. 1985 Jan 16;126(1):220–226. doi: 10.1016/0006-291x(85)90594-7. [DOI] [PubMed] [Google Scholar]
  21. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Seidah N. G., Arbatti N. J., Rochemont J., Sheth A. R., Chrétien M. Complete amino acid sequence of human seminal plasma beta-inhibin. Prediction of post Gln-Arg cleavage as a maturation site. FEBS Lett. 1984 Oct 1;175(2):349–355. doi: 10.1016/0014-5793(84)80766-8. [DOI] [PubMed] [Google Scholar]
  23. Steiner D. F., Quinn P. S., Chan S. J., Marsh J., Tager H. S. Processing mechanisms in the biosynthesis of proteins. Ann N Y Acad Sci. 1980;343:1–16. doi: 10.1111/j.1749-6632.1980.tb47238.x. [DOI] [PubMed] [Google Scholar]
  24. Wagh P. V., Bahl O. P. Sugar residues on proteins. CRC Crit Rev Biochem. 1981;10(4):307–377. doi: 10.3109/10409238109113602. [DOI] [PubMed] [Google Scholar]
  25. Watson M. E. Compilation of published signal sequences. Nucleic Acids Res. 1984 Jul 11;12(13):5145–5164. doi: 10.1093/nar/12.13.5145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. de Jong F. H., Robertson D. M. Inhibin: 1985 update on action and purification. Mol Cell Endocrinol. 1985 Sep;42(2):95–103. doi: 10.1016/0303-7207(85)90096-6. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES