Advertisement

Journal of Protein Chemistry

, Volume 8, Issue 5, pp 647–652 | Cite as

Primary structure of hemoglobin from gray partridge (Francolinus pondacerianus, Galliformes)

  • Atiya Abbasi
  • Zafar H. Zaidi
Articles

Abstract

The complete amino acid sequence of the αA-chain of major hemoglobin component from gray partridgeFrancolinus pondacerianus is presented. The major component HbA accounts for 75% of the total hemolysate. Separation of the globin subunits was achieved by ion-exchange chromatography on CM-Cellulose in 8 M urea. The sequence was studied by automatic Edman degradation of the native chain and its tryptic peptides in a gas-phase sequencer. The phylogenetic relationship of Galliformes with other avian orders is discussed.

Key words

hemoglobin primary structure gray partridge evolution 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Abbasi, A., Wells, R. G. M., Brittian, T., and Braunitzer, G. (1988).Biol. Chem. Hoppe Seyler 369, 755–764.Google Scholar
  2. Alter, B. P., Goff, S. C., Efremov, G. D., Gravely, M. E., and Huisman, T. H. J. (1980).Br. J. Haematol. 44, 527–534.Google Scholar
  3. Bauer, H., Braunitzer, G., Oberthur, W., Kosters, J., and Grimm, F. (1985).Biol. Chem. Hoppe Seyler 366, 1141–1148.Google Scholar
  4. Braunitzer, G., and Godovac, J. (1982).Hoppe Seyler's Z. Physiol. Chem. 363, 229–238.Google Scholar
  5. Clegg, J. B., Naughton, M. A., and Weatherall, D. J. (1966).J. Mol. Biol. 19, 91–108.Google Scholar
  6. Edman, P., and Begg, G. (1967).Eur. J. Biochem. 1, 80–91.Google Scholar
  7. Fermi, G., and Perutz, M. F. (1981). InAtlas of Molecular Structures in Biology, Part 2: Hemoglobin and Myoglobin (Phillips, D. C. and Richards, F. M., eds.), Clarendon Press, Oxford, p. 102.Google Scholar
  8. Erbil, C., and Niessing, J. (1982).Gene 20, 211–217.Google Scholar
  9. Godovac-Zimmermann, J., and Braunitzer, G. (1983).Hoppe Seyler's Z. Physiol. Chem. 364, 665–674.Google Scholar
  10. Godovac-Zimmermann, J., and Braunitzer, G. (1984).Hoppe Seyler's Z. Physiol. Chem. 365, 437–443.Google Scholar
  11. Godovac-Zimmermann, J., and Braunitzer, G. (1984).Hoppe Seyler's Z. Physiol. Chem. 365, 1107–1113.Google Scholar
  12. Godovac-Zimmermann, J., and Braunitzer, G. (1985).Biol. Chem. Hoppe Seyler 366, 503–508.Google Scholar
  13. Godovac-Zimmerman, J., Kosters, J., Braunitzer, G., and Goltenboth, R. (1988).Biol. Chem. Hoppe Seyler 369, 341–348.Google Scholar
  14. Hewick, R. M., Hunkapiller, M. W., Hood, L. E., and Dreyer, W. J. (1981).J. Biol. Chem. 256, 7990–7997.Google Scholar
  15. Hiebl, I., Schneeganss, D., Grimm, F., Kosters, J., and Braunitzer, G. (1987).Biol. Chem. Hoppe Seyler 368, 11–18.Google Scholar
  16. Hiebl, I., Kosters, J., and Braunitzer, G. (1987).Biol. Chem. Hoppe Seyler 368, 333–342.Google Scholar
  17. Hiebl, I., Weber, R. E. Schneeganss, D., Kosters, J., and Braunitzer, G. (1988).Biol. Chem. Hoppe Seyler 369, 217–232.Google Scholar
  18. Hirs, C. H. W. (1967).Methods Enzymol. 11, 216–222.Google Scholar
  19. Isaacks, R. E. and Harkness, D. R. (1980).Am. Zool. 20, 115–129.Google Scholar
  20. Islam, A., Beg, O. U., Persson, B., Zaidi, Z. H. and Jornvall, H. (1988).J. Protein. Chem. 7, 561–569.Google Scholar
  21. Jolles, J., Schoentgen, F., Jolles, P., Prager, E. M., and Wilson, A. C. (1976).J. Mol. Evol. 8, 59–78.Google Scholar
  22. Korinna, H. (1988). Ph.D. thesis, Universitaet Muenchen.Google Scholar
  23. Kratzin, H., Yang, C., Krusche, J. U., and Hilschman, N. (1980).Hoppe Seyler's Z. Physiol. Chem. 361, 1591–1598.Google Scholar
  24. Knochel, W., Wittig, B., Wittig, S., John, M. E., Grundmann, U., Oberthur, W., Godovac, J., and Braunitzer, G. (1982).Nature (London) 295, 710–712.Google Scholar
  25. Lutz, P. L. (1980).Am. Zool. 20, 187–198.Google Scholar
  26. Maurer, H. R. (1971).Disc Electrophoresis, Walter de Gruyter, Berlin.Google Scholar
  27. Nothum, R. (1988). Ph.D. thesis, Universitaet Muenchen.Google Scholar
  28. Oberthur, W., Voelter, W., and Braunitzer, G. (1980).Hoppe Seyler's Z. Physiol. Chem. 361, 969–975.Google Scholar
  29. Oberthur, W., Braunitzer, G., and Kalas, S. (1981).Hoppe Seyler's Z. Physiol. Chem. 362, 1102–1112.Google Scholar
  30. Oberthur, W., Braunitzer, G., and Wurdinger, I. (1982).Hoppe Seyler's Z. Physiol. Chem. 363, 581–590.Google Scholar
  31. Oberthur, W., Godovac-Zimmermann, J., Braunitzer, G., and Wiesner, H. (1982).Hoppe Seyler's Z. Physiol. Chem. 363, 777–787.Google Scholar
  32. Oberthur, W., Braunitzer, G., Bauman, R., and Wright, P. G. (1983).Hoppe Seyler's Z. Physiol. Chem. 364, 119–134.Google Scholar
  33. Oberthur, W., Wiesner, H., and Braunitzer, G. (1983).Hoppe Seyler's Z. Physiol. Chem. 364, 51–59.Google Scholar
  34. Oberthur, W., Braunitzer, G., Grimm, F., and Kosters J. (1983).Hoppe Seyler's Z. Physiol. Chem. 364, 851–858.Google Scholar
  35. Oberthur, W., and Braunitzer, G. (1984).Hoppe Seyler's Z. Physiol. Chem. 365, 159–173.Google Scholar
  36. Perutz, M. F. (1979).Ann. Rev. Biochem. 48, 327–386.Google Scholar
  37. Prager, E. M., and Wilson, A. C. (1976).J. Mol. Evol. 9, 43–57.Google Scholar
  38. Rossi-Fanelli, A., and Antonini, E. (1958).Biochim. Biophys. Acta 30, 608–615.Google Scholar
  39. Schneeganss, D., Braunitzer, G., Oberthur, W., Kosters, J., and Grimm, F. (1985).Biol. Chem. Hoppe Seyler 366, 893–899.Google Scholar
  40. Sultana, C., Abbasi, A., and Zaidi, Z. H. (1988). InProtein Structure Function Relationship, (Zaidi, Z. H., ed), Elsevier Science Publishers B.V., Amsterdam, Holland, pp. 213–223.Google Scholar
  41. Wood, S. C. and Lenfant, C. (1979). InEvolution of Respiratory Processes, Marcel Dekker, Inc., New York, pp. 193–223.Google Scholar

Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • Atiya Abbasi
    • 1
  • Zafar H. Zaidi
    • 1
  1. 1.HEJ Research Institute of ChemistryUniversity of KarachiKarachiPakistan

Personalised recommendations