Journal of Protein Chemistry

, Volume 19, Issue 2, pp 105–116

New Genetic Variants Identified in Donkey's Milk Whey Proteins

Authors

  • Maryse Herrouin
    • EURL François Ballestra
  • Daniel Mollé
    • INRA, Laboratoire de Recherche en Technologie Laitière
  • Jacques Fauquant
    • INRA, Laboratoire de Recherche en Technologie Laitière
  • François Ballestra
    • EURL François Ballestra
  • Jean-Louis Maubois
    • INRA, Laboratoire de Recherche en Technologie Laitière
  • Joëlle Léonil
    • INRA, Laboratoire de Recherche en Technologie Laitière
Article

DOI: 10.1023/A:1007078415595

Cite this article as:
Herrouin, M., Mollé, D., Fauquant, J. et al. J Protein Chem (2000) 19: 105. doi:10.1023/A:1007078415595

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 spectrometryprotein sequencewhey proteindonkey milk

Copyright information

© Plenum Publishing Corporation 2000