Journal of Protein Chemistry

, Volume 19, Issue 2, pp 105–116

New Genetic Variants Identified in Donkey's Milk Whey Proteins

  • Maryse Herrouin
  • Daniel Mollé
  • Jacques Fauquant
  • François Ballestra
  • Jean-Louis Maubois
  • Joëlle Léonil
Article

Abstract

Novel genetic variants for donkey milk lysozyme and β-lactoglobulins I and II have been identified by the combined use of peptide mass mapping and sequencing by tandem mass spectrometry in association with database searching. The novel donkey lysozyme variant designated as lysozyme B (Mr 14,631 Da) differed in three amino acid exchanges, N49 → D, Y52 → S, and S61 → N, from the previously published sequence. Three novel genetic variants for donkey β-lactoglobulins were identified. One of them is a type β-lactoglobulin I with three amino acid exchanges at E36 → S, S97 → T, and V150 → I (β-lactoglobulin I B, Mr 18,510 Da). The two others are type β-lactoglobulins II with two amino acid exchanges at C110 → P and M118 → T (β-lactoglobulin II B, Mr 18,227 Da) and with three amino acid exchanges at D96 → E, C110 → P, and M118 → T (β-lactoglobulin II C, Mr 18,241 Da). All these primary structures are closely related to those of homologous proteins in horse milk (percent identity >96%).

Mass spectrometry protein sequence whey protein donkey milk 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

REFERENCES

  1. Ali, S., McClenaghan, M., Simons, J. P. and Clark, A. J. (1990). Gene 91, 201–207.Google Scholar
  2. Barnett, D. A., Ells, B., Guevremont, R., and Purves, R. W. (1999). Am. Soc. Mass Spectrom. 10, 1279–1284.Google Scholar
  3. Bell, K., McKenzie, H. A., Muller, V., and Shaw, D. C. (1980). Mol. Cell. Biochem. 29, 3–9.Google Scholar
  4. Bell, K., McKenzie, H. A., Muller, V., Rogers, C., and Shaw, D. C. (1981). Comp. Biochem. Physiol. 68, 225–236.Google Scholar
  5. Brot, N., and Weissbach, H. (1983). Arch. Biochem. Biophys. 223, 271–281.Google Scholar
  6. Carr, S. A., Hemling, M. E., Bean, M. F., and Roberts, G. D. (1992). Anal. Chem. 63, 2802–2824.Google Scholar
  7. Conti, A., Godovac-Zimmermann, J., Liberatori, J., Braunitzer, G., and Minori, D. (1984). Hoppe-Seyler's Z. Physiol. Chem. 365, 1393–1401.Google Scholar
  8. Conti, A., Godovac-Zimmermann, J., Liberatori, J., and Braunitzer, G. (1985). Biol. Chem. Hoppe-Seyler 366, 601–608.Google Scholar
  9. Conti, A., Napolitano, L., Lai, P., Pinna, W., and Godovac-Zimmermann, J. (1989). Milchwissenschaft 44, 138–141.Google Scholar
  10. Doreau, M. (1991). Prod. Anim. 4, 297–302.Google Scholar
  11. Eigel, W. N., Butler, J. E., Ernstrom, C. A., Farrell, H. M. J., Harwalkar, V. R., Jenness, R., and Whitney, R. (1984). J. Dairy Sci. 67, 1599–1631.Google Scholar
  12. El Salam, A., Farag, S. I., El Dein, H. F., Mahfouz, M. B., and El-Etriby, H. M. (1992). In Proceedings 5th Egyptian Conference Dairy Science and Technology, pp. 281–287.Google Scholar
  13. Erhardt, G., Godovac-Zimmermann, J., and Conti, A. (1989). Biol. Chem. Hoppe-Seyler 370, 757–762.Google Scholar
  14. Gaskell, S. J. (1997). J. Mass Spectrom. 32, 677–688.Google Scholar
  15. Giufrida, M. G., Cantisani, A., Napolitano, L., Conti, A., and Godovac-Zimmermann, J. (1992). Biol. Chem. Hoppe-Seyler 373, 931–935.Google Scholar
  16. Godovac-Zimmermann, J., Shaw, D. C., Conti, A., and McKenzie, H. A. (1987). Biol. Chem. Hoppe-Seyler 368, 427–433.Google Scholar
  17. Godovac-Zimmermann, J., Conti, A., James, L., and Napolitano, L. (1988a). Biol. Chem. Hoppe-Seyler 369, 171–179.Google Scholar
  18. Godovac-Zimmermann, J., Conti, A., and Napolitano, L. (1988b). Biol. Chem. Hoppe-Seyler 369, 1109–1115.Google Scholar
  19. Godovac-Zimmermann, J., Conti, A., Sheil, M., and Napolitano, L. (1990). Biol. Chem. Hoppe-Seyler 371, 871–879.Google Scholar
  20. Grosclaude, F. (1988). Prod. Anim. 1, 5–17.Google Scholar
  21. Halliday, J. A., Bell, K., McKenzie, H. A., and Shaw, D. C. (1990). Comp. Biochem. Physiol. 95B, 773–779.Google Scholar
  22. Halliday, J. A., Bell, K., and Shaw, D. C. (1991). Biochim. Biophys. Acta 1077, 25–30.Google Scholar
  23. Halliday, J. A., Bell, K., Mcandrew, K., and Shaw, D. C. (1993). Protein Seq. Data Anal. 5, 201–205.Google Scholar
  24. Hollecker, M. (1990). Protein Structure: A Practical Approach, IRL Press, Oxford, pp. 145–153.Google Scholar
  25. Iacono, G., Carroccio, A., Cavataio, F., Montalto, G., Soresi, M., and Balsamo, V. (1992). J. Pediat. Gastroenterol. Nutr. 14, 177–181.Google Scholar
  26. Jakob, E. (1994). FIL-IDF 298, 17–27.Google Scholar
  27. Jakob, E., and Puhan, Z. (1992). Int. Dairy J. 2, 157–178.Google Scholar
  28. Laemmli, U. K. (1970). Nature 227, 680–685.Google Scholar
  29. Mann, M., Hojrup, P., and Roepstorff, P. (1993). Biol. Mass Spectrom. 22, 338–345.Google Scholar
  30. Manneberg, M., Lahm, H. W., and Fountoulakis, M. (1995). Anal. Biochem. 224, 122–127.Google Scholar
  31. McKenzie, H. A., and Shaw, D. C. (1985). Biochem. Int. 10, 23–31.Google Scholar
  32. North, A. C. T. (1989). Int. J. Biol. Macromol. 11, 56–58.Google Scholar
  33. Pagliarini, E., Solaroli, G., and Peri, C. (1993). Ital. J. Food Sci. 4, 323–332.Google Scholar
  34. Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, R., Jones, T. A., et al. (1986). Nature 324, 383–385.Google Scholar
  35. Preaux, G., Braunitzer, G., Schrank, B., and Stangl, A. (1979). Hoppe-Seyler's Z. Physiol. Chem. 360, 1595–1604.Google Scholar
  36. Roepstorff, P., and Fohlman, J. (1984). Biomed. Mass Spectrom. 11, 601.Google Scholar
  37. Smith, J. B., Thevenon-Emerie, G., Smith, D. L., and Green, B. (1991). Anal. Biochem. 193, 118–124.Google Scholar
  38. Solaroli, G., Pagliarini, E., and Peri, C. (1993). Ital. J. Food Sci., 1, 3–10.Google Scholar
  39. Tunon, P., and Johansson, K. E. (1984). J. Biochem. Biophys. Meth. 9, 171–179.Google Scholar

Copyright information

© Plenum Publishing Corporation 2000

Authors and Affiliations

  • Maryse Herrouin
    • 1
  • Daniel Mollé
    • 2
  • Jacques Fauquant
    • 2
  • François Ballestra
    • 1
  • Jean-Louis Maubois
    • 2
  • Joëlle Léonil
    • 3
  1. 1.EURL François BallestraSAINT-RAPHAËLFrance
  2. 2.INRA, Laboratoire de Recherche en Technologie LaitièreRennes CedexFrance
  3. 3.INRA, Laboratoire de Recherche en Technologie LaitièreRennes CedexFrance

Personalised recommendations