Journal of Protein Chemistry

, Volume 5, Issue 6, pp 379–384 | Cite as

31P nuclear magnetic resonance study of enzymatically phosphorylated glycophorin A

  • Karen A. Culp
  • Kilian Dill


Glycophorin A was phosphorylated using protein kinases and the new protein was investigated using31P NMR spectroscopy. Most of these ∼30 moles of phosphate were found to be attached to Ser and Thr. Some of these phosphate residues appear to be affected by the carbohydrate residues present. The phosphorylated protein appears to be in a severe state of aggregation, with the degree of aggregationpH-dependent.

Key words

glycophorin A 31P nuclear magnetic resonance spectroscopy phosphorylation phosphoproteins 


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  1. Armitage, I. M., Shapiro, D. L., Furthmayr, H., and Marchesi, V. T. (1977).Biochemistry 16, 1317–1320.Google Scholar
  2. Avruch, J., and Fairbanks, G. (1974).Biochemistry 13, 5507–5521.Google Scholar
  3. Carter, R. D., Lannom, H. K., and Dill, K. (1985).Biochim. Biophys. Acta 845, 396–402.Google Scholar
  4. Clari, G., and Moret, V. (1985).Mol. Cell. Biochem. 68, 181–187.Google Scholar
  5. Daman, D., and Dill, K. (1983).Carbohydr. Res. 111, 205–213.Google Scholar
  6. Davis, M. D., Edmundson, D. E., and Muller, F. (1984).Eur. J. Biochem. 145, 237–243.Google Scholar
  7. Dill, K., and Carter, R. D. (1986).Prog. NMR Spectrosc. 18, 307–326.Google Scholar
  8. Dzandu, J. K., and Johnson, R. M. (1980).J. Biol. Chem. 255, 6382–6386.Google Scholar
  9. Dzandu, J. K., Deh, M. E., and Kienu, P. (1985).Biochem. Biophys. Res. Commun. 122, 878–884.Google Scholar
  10. Furthmayr, H., and Marchesi, V. T. (1983).Meth. Enzymol. 96, 268–280.Google Scholar
  11. Gorenstein, D. G., ed. (1984).Phosphorus-31 NMR Principles and Applications, Academic Press, New York.Google Scholar
  12. Guthrow, C. E., Allen, J. E., and Rasmussen, H. (1972).J. Biol. Chem. 247, 8145–8153.Google Scholar
  13. Hardy, R. E., Batstone-Cunningham, R. L., and Dill, K. (1983).Arch. Biochem. Biophys. 222, 222–230.Google Scholar
  14. Horne, W. C., and Marchesi, V. T. (1985).J. Biol. Chem. 260, 9073–9076.Google Scholar
  15. Hosey, M. M., and Tao, M. J. (1972).J. Supramol. Struct. 6, 61–75.Google Scholar
  16. Hosey, M. M., and Tao, M. (1976).Biochemistry 15, 1561–1568.Google Scholar
  17. Hosey, M. M., and Tao, M. (1977).J. Biol. Chem. 252, 102–109.Google Scholar
  18. Johnson, R. M., McGowan, M. W., Morse II, P. D., and Dzandu, J. K. (1982).Biochemistry 21, 3599–3604.Google Scholar
  19. Marchesi, V. T. (1979).Semin. Hematol. 16, 3–20.Google Scholar
  20. Miller, M. S., Mas, M. T., and White III, H. B. (1984).Biochemistry 23, 569–576.Google Scholar
  21. Plutt, D. A., Hosey, M. M., and Tao, M. (1978).Eur. J. Biochem. 82, 333–337.Google Scholar
  22. Rubin, C. S., and Rosen, O. M. (1973).Biochem. Biophys. Res. Commun. 50, 421–429.Google Scholar
  23. Shapiro, D. L., and Marchesi, V. T. (1977).J. Biol. Chem. 252, 508–517.Google Scholar
  24. Shiba, T., Akiyama, T., Kadowaki, T., Fukami, Y., Tsuji, T., Osawa, T., Kasuga, M., and Takaku, F. (1986).Biochem. Biophys. Res. Commun. 135, 720–727.Google Scholar
  25. Waxman, L. (1979).Arch. Biochem. Biophys. 195, 300–314.Google Scholar
  26. Weller, M. (1979).Protein Phosphorylation, Pion, London.Google Scholar
  27. Williams, R. O. (1972).Biochem. Biophys. Res. Commun. 42, 671–678.Google Scholar
  28. Williams, S. P., Sykes, B. D., and Bridger, W. A. (1985).Biochemistry 24, 5527–5531.Google Scholar

Copyright information

© Plenum Publishing Corporation 1986

Authors and Affiliations

  • Karen A. Culp
    • 1
  • Kilian Dill
    • 1
  1. 1.Department of ChemistryClemson UniversityClemson

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