Journal of Protein Chemistry

, Volume 10, Issue 2, pp 145–149 | Cite as

Primary structure of hemoglobin β-chain fromColumba livia (gray wild pigeon)

  • Chand Sultana
  • Atiya Abbasi
  • Zafar H. Zaidi
Article

Abstract

Primary structure of β-chain of pigeon is presented. It was determined by amino acid sequence analysis of intact β-chain and its peptides obtained by the enzymatic and chemical cleavage. Comparison of amino acid sequence of the chain with other available data shows β 14 Ile, β61 Lys, and β113 Ile as residues specific to pigeon. One important replacement at α1β1 contact is β55 Met→Ser.

Key words

Primary structure β-chain hemoglobin Columbiformes evolution 

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References

  1. Bauer, H., Braunitzer, G., Oberthur, W., Kosters, J., and Grimm, F. (1985).Biol. Chem. Hoppe-Seyler 366, 1141–1148.Google Scholar
  2. Braunitzer, G., Gehring-Muller, R., Hilschmann, M., Hilse, K., Hobom, G., Rudloff, V., and Wittmann-Liebold, B. (1961).Hoppe-Seyler's Z. Physiol. Chem. 325, 283–286.Google Scholar
  3. Braunitzer, G., and Godovac-Zimmermann, J. (1982).Hoppe-Seyler's Z. Physiol. Chem. 363, 229–238.Google Scholar
  4. Dawson, T. T. J., and Evans, J. V. (1966).Am. J. Physiol. 2210, 1021–1025.Google Scholar
  5. Godovac-Zimmermann, J., and Braunitzer, G. (1983).Hoppe-Seyler's Z. Physiol. Chem. 364, 665–674.Google Scholar
  6. Godovac-Zimmermann, J., and Braunitzer, G. (1984).Hoppe-Seyler's Z. Physiol. Chem. 365, 1107–1113.Google Scholar
  7. Godovac-Zimmermann, J., and Braunitzer, G. (1985).Biol. Chem. Hoppe-Seyler 366, 503–508.Google Scholar
  8. Godovac-Zimmermann, J., Koster, J., and Braunitzer, G. (1988).Biol. Chem. Hoppe-Seyler,369, 741–748.Google Scholar
  9. Godovac-Zimmermann, J., and Braunitzer, G. (1984).Hoppe-Seyler's Z. Physiol. Chem. 365, 437–443.Google Scholar
  10. Hiebl, I., Braunitzer, G., and Schneeganss, D. (1987).Biol. Chem. Hoppe-Seyler 368, 1559–1569.Google Scholar
  11. Hiebl, I., Kosters, J., and Braunitzer, G. (1987).Biol. Chem. Hoppe-Seyler 368, 333–342.Google Scholar
  12. Hiebl, I., Schneeganss, D., Grimm, F., Kosters, J., and Braunitzer, G. (1987).Biol. Chem. Hoppe-Seyler 368, 11–18.Google Scholar
  13. Hiebl, I., Weber, R. E., Schneeganss, D., Kosters, J., and Braunitzer, G. (1988).Biol. Chem. Hoppe-Seyler 369, 217–232.Google Scholar
  14. Huber, K., Braunitzer, G., Schneeganss, D., Kosters, J., and Grimm, F. (1988).Biol. Chem. Hoppe-Seyler 369, 1251–1258.Google Scholar
  15. Huber, K., Braunitzer, G., Schneeganss, D., Kosters, J., and Grimm, F. (1988).Biol. Chem. Hoppe-Seyler 369, 513–519.Google Scholar
  16. Islam, A., Beg, O. U., Pervsson, B., Zaidi, Z. H., and Jornvall, H. (1988).J. Prot. Chem. 7, 561–569.Google Scholar
  17. Kleinschmidt, T., and Sgouros, J. G. (1987).Biol. Chem. Hoppe-Seyler 368, 579–615.Google Scholar
  18. Maita, T., Mizuno, K., and Matsuda, G. (1975).J. Biochem. 78, 1311–1319.Google Scholar
  19. Matsuda, G., Maita, T., Mizuno, K., and Ota, H. (1973).Comp. Biochem. Physiol. 44A, 711–718.Google Scholar
  20. Nothum, R., Braunitzer, G., Hiebl, I., Kosters, J., and Schneeganss, D. (1989).Biol. Chem. Hoppe-Seyler 370, 309–316.Google Scholar
  21. Oberthur, W., Braunitzer, G., and Wurdinger, I. (1982).Hoppe-Seyler's Z. Physiol. Chem. 363, 581–590.Google Scholar
  22. Oberthur, W., Braunitzer, G., and Kalas, S. (1981).Hoppe-Seyler's Z. Physiol. Chem. 362, 1101–1112.Google Scholar
  23. Oberthur, W., Godovac-Zimmermann, J., and Braunitzer, G. (1982).Hoppe-Seyler's Z. Physiol. Chem. 363, 777–787.Google Scholar
  24. Oberthur, W., Braunitzer, G., Baumann, R., and Wright, P. G. (1983).Hoppe-Seyler's Z. Physiol. Chem. 364, 119–134.Google Scholar
  25. Oberthur, W., Braunitzer, G., Grimm, F., and Kosters, J. (1983).Hoppe-Seyler's Z. Physiol. Chem. 364, 851–858.Google Scholar
  26. Oberthur, W., Wiesner, H., and Braunitzer, G. (1983).Hoppe-Seyler's Z. Physiol. Chem. 364, 51–59.Google Scholar
  27. Oberthur, W., and Braunitzer, G. (1984).Hoppe-Seyler's Z. Physiol. Chem. 365, 159–173.Google Scholar
  28. Paul, C., Vandecasserie, C., Fraboni, A., Depreter, J., Leonis, J., and Schnek, A. G. (1977). InInteraction Moleculaires de l'Hemoglobine, Colloque de l'INSERM Paris, Pub. 1978 (Labie, D., Poyart, F., and Rosa, J., eds.), INSERM, Paris, pp. 183–200.Google Scholar
  29. Perrins, C. M., and Middleton, A. L. A. (1985).The Encyclopaedia of Birds, George Allen and Unwin, London.Google Scholar
  30. Schneeganss, D., Braunitzer, G., Oberthur, W., Kosters, J., and Grimm, F. (1985).Biol. Chem. Hoppe-Seyler 366, 893–899.Google Scholar
  31. Sultana, C., Abbasi, A., and Zaidi, Z. H. (1989).J. Prot. Chem. 8, 629–646.Google Scholar
  32. Swan, L. W. (1970).Nat. Hist. 79, 68–75.Google Scholar

Copyright information

© Plenum Publishing Corporation 1991

Authors and Affiliations

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

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