Journal of Protein Chemistry

, Volume 1, Issue 4, pp 263–280 | Cite as

Structural studies on equine chorionic gonadotropin

  • Darrell N. Ward
  • William T. Moore
  • B. Daniel Burleigh
Article
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Abstract

The amino acid sequence of the α subunit of equine chorionic gonadotropin (eCG, also pregnant mare serum gonadotropin, PMSG) has been determined. Overlapping peptides from tryptic and chymotrypic digests were isolated by a two-dimensional peptide mapping technique and sequenced by the Edman procedure. The proposed amino acid sequence of eCG α is:
(**Denotes carbohydrate attachment points.) This sequence differs significantly from that proposed by Rathnamet al. (1978) for equine follitropin α subunit; in particular, their sequence lacked the first fourteen residues.
For the β subunit we have placed in sequence 104 amino acid residues by direct sequence determination and peptide overlap procedures; in addition, 37 residues have been placed provisionally by homology with the human chorionic gonadotropin (hCG) sequence and composition and/or sequence data for the peptides isolated in the present studies. Difficulties in the procurement of the hormone have stalled completion of the β-subunit amino acid sequence determination. The data now available indicate that eCG β-subunit is highly homologous to hCG β subunit and the β subunits of luteinizing hormone from the pituitary gland of the several species so far described. The proposed partial sequence of eCG β is:

Key words

chorionic gonadotropin equine structure chorionic gonadotropin alpha and beta subunits chorionic gonadotropin amino acid sequence pregnant Mare Serum gonadotropin 
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References

  1. Bellisario, R., Carlsen, R. B., and Bahl, O. P. (1973).J. Biol. Chem. 248, 6796–6809.Google Scholar
  2. Birken, S., and Canfield, R. E. (1977).J. Biol. Chem. 252, 5386–5392.Google Scholar
  3. Blomback, B. (1967). In (Colowick, S. P., and Kaplan, N. O. (eds.),Methods in Enzymology, Vol. II, Academic Press, New York, pp. 398–411.Google Scholar
  4. Brown, F. F., Parsons, T. F., Sigman, D. S., and Pierce, J. G. (1979).J. Biol. Chem. 254, 4335–4338.Google Scholar
  5. Burleigh, B. D., Liu, W-K., and Ward, D. N. (1976).J. Biol. Chem. 251, 308–315.Google Scholar
  6. Carlsen, R. B., Bahl, O. P., and Swaminathan, N. (1973).J. Biol. Chem. 248, 6810–6825.Google Scholar
  7. Christakos, S., and Bahl, O. (1979).J. Biol. Chem. 254, 4253–4261.Google Scholar
  8. Closset, J., Hennen, G., and Lequin, R. M. (1973).FEBS Lett. 29, 97–100.Google Scholar
  9. Closset, J., Maghuin-Rogister, C., Hennen, G., and Strosberg, A. D. (1978).Eur. J. Biochem. 86, 115–120.Google Scholar
  10. Cole, R. D. (1967). In Colowick, S. P., and Kaplan, N. O. (eds.),Methods in Enzymology, Vol. II, Academic Press, New York, pp. 315–317.Google Scholar
  11. Combarnous, Y. and Henge, M.-H. (1981).J. Biol. Chem. 256, 9567–9572.Google Scholar
  12. Edelhoch, H. (1967).Biochemistry 6, 1948–1954.Google Scholar
  13. Edge, A. S. B., Faltynek, C. R., Hof, L., Reichert, L. E., Jr., and Weber, P. (1981).Anal. Biochem. 118, 131–136.Google Scholar
  14. Fujiki, Y., Rathnam, P., and Saxena, B. B. (1978).J. Biol. Chem. 253, 5363–5368.Google Scholar
  15. Fujiki, Y., Rathnam, P., and Saxena, B. B. (1980).Biochim. Biophys. Acta 624, 428–435.Google Scholar
  16. Hartley, B. S. (1980).Biochem. J. 119, 805–822.Google Scholar
  17. Hugli, T. E., and Moore, S. (1972).J. Biol. Chem. 247, 2828–2834.Google Scholar
  18. Keutmann, H. T., and Williams, R. M. (1977).J. Biol. Chem. 252, 5393–5397.Google Scholar
  19. Keutmann, H. T., Williams, R. M., and Ryan, R. J. (1979).Biochem. Biophys. Res. Commun. 90, 842–847.Google Scholar
  20. Landefeld, T. D., Grimek, H. J., and McShan, W. H. (1972).Biochem. Biophys. Res. Commun. 46, 463–469.Google Scholar
  21. Liao, T.-H., and Pierce, J. G. (1970).J. Biol. Chem. 245, 3275–3281.Google Scholar
  22. Liao, T.-H., and Pierce, J. G. (1971).J. Biol. Chem. 246, 850–865.Google Scholar
  23. Liao, T.-H., Hennen, G., Howard, S. M., Shome, B., and Pierce, J. J. (1969).J. Biol. Chem. 244, 6458–6467.Google Scholar
  24. Liu, W.-K., and Meinhofer, J. (1968).Biochem. Biophys. Res. Commun. 31, 467–473.Google Scholar
  25. Liu, W.-K., Nahm, H. S., Sweeney, C. M., Lamkin, W. M., Baker, H. N., and Ward, D. N. (1972a).J. Biol. Chem. 247, 4351–4364.Google Scholar
  26. Liu, W.-K., Nahm, H. S., Sweeney, C. M., Holcomb, G. N., and Ward, D. N. (1972b).J. Biol. Chem. 247, 5365–4381.Google Scholar
  27. Maghuin-Rogister, G., and Hennen, G. (1973).Eur. J. Biochem. 39 235–253.Google Scholar
  28. Maghuin-Rogister, G., Combarnous, Y., and Hennen, G. (1973).Eur. J. Biochem. 39, 255–263.Google Scholar
  29. Maghuin-Rogister, G., Hennen, G., and Closset, J. (1976).Eur. J. Biochem. 61, 157–163.Google Scholar
  30. Malsky, M. L., Bullock, D. W., Willard, J. J., and Ward, D. N. (1979).J. Biol. Chem. 254, 1580–1585.Google Scholar
  31. Moore, W. T., Jr., and Ward, D. N. (1980a).J. Biol. Chem. 255, 6923–6929.Google Scholar
  32. Moore, W. T., Jr., and Ward, D. N. (1980b).J. Biol. Chem. 255, 6930–6936.Google Scholar
  33. Moore, W. T., Jr., Ward, D. N., and Burleigh, B. D. (1979).Fed. Proc. 38, 462–463.Google Scholar
  34. Moore, W. T., Jr., Burleigh, B. D., and Ward, D. N. (1980). In Segal, S. J. (ed.),Chorionic Gonadotropin, Plenum Press, New York, pp. 89–126.Google Scholar
  35. Morgan, F. J., Birken, S., and Canfield, R. E. (1973).Molec. Cell. Biochem. 2, 97–99.Google Scholar
  36. Mort, A. J., and Lamport, D. T. A. (1977).Anal. Biochem. 82, 289–309.Google Scholar
  37. Mueller, J. M., Pierce, J. G., Davoll, H., and duVigneaud, V. (1951).J. Biol. Chem. 191, 309–313.Google Scholar
  38. Nuti, L. C., Grimek, H. J., Braselton, W. E., and McShan, W. H. (1972).Endocrinology 91, 1418–1422.Google Scholar
  39. Offord, R. E. (1966).Nature 211, 591–593.Google Scholar
  40. Papkoff, H., Bewley, T. A., and Ramachandran, J. (1978).Biochim. Biophys. Acta 532, 185–194.Google Scholar
  41. Pierce, J. G., and Parsons, T. F. (1981).Annu. Rev. Biochem. 50, 465–495.Google Scholar
  42. Rathnam, P., and Saxena, B. B. (1975).J. Biol. Chem. 250, 6735–6746.Google Scholar
  43. Rathnam, P., Fujiki, Y., Landefeld, T. D., and Saxena, B. B. (1978).J. Biol. Chem. 253, 5355–5362.Google Scholar
  44. Sairam, M. R. (1981a).Biochem. J. 197, 535–540.Google Scholar
  45. Sairam, M. R. (1981b).Biochem. J. 197, 541–546.Google Scholar
  46. Sairam, M. R., and Li, C.-H. (1973).Biochem. Biophys. Res. Commun. 54, 426–431.Google Scholar
  47. Sairam, M. R., and Li, C.-H. (1975).Biochim. Biophys. Acta 412, 70–81.Google Scholar
  48. Sairam, M. R., Samy, T. S. A., Papkoff, H., and Li, C.-H. (1972a).Arch. Biochem. Biophys. 153, 572–586.Google Scholar
  49. Sairam, M. R., Papkoff, H., and Li, C.-H. (1972b).Biochem. Biophys. Res. Commun. 48, 530–537.Google Scholar
  50. Saxena, B. B., and Rathnam, P. (1976).J. Biol. Chem. 251, 993–1005.Google Scholar
  51. Shome, B., and Parlow, A. F. (1973a).J. Clin. Endocrinol. Metab. 36, 618–621.Google Scholar
  52. Shome, B., and Parlow, A. F. (1973b). In 55th National Endocrine Meeting, Abstract A-60, No. 22, Chicago, Illinois.Google Scholar
  53. Shome, B., and Parlow, A. F. (1974a).J. Clin. Endocrinol. Metab. 39, 199–202.Google Scholar
  54. Shome, B., and Parlow, A. F. (1974b).J. Clin. Endocrinol. Metab. 39, 203–205.Google Scholar
  55. Ward, D. N., Reichert, L. E., Jr., Liu, W.-K., Nahm, H. S., and Lamkin, W. M. (1972). In Saxena, B. B., Beling, C. G., and Gandy, H. M. (eds.),Gonadotropins, Wiley, New York, pp. 132–143.Google Scholar
  56. Ward, D. N., Reichert, L. E., Jr., Liu, W.-K., Nahm, H. S., Hsia, J., Lamkin, W. M., and Jones, N. S. (1973).Recent Prog. Horm. Res. 29, 533–561.Google Scholar

Copyright information

© Plenum Publishing Corporation 1982

Authors and Affiliations

  • Darrell N. Ward
    • 1
  • William T. Moore
    • 1
  • B. Daniel Burleigh
    • 2
  1. 1.M. D. Anderson Hospital and Tumor Institute, Department of BiochemistryThe University of Texas System Center CenterHouston
  2. 2.International Minerals & Chemical Corp.Terre Haute

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