Amino acid sequence and crystal structure of buffalo α-lactalbumin

V. Calderone, M. G. Giuffrida, D. Viterbo, L. Napolitano, D. Fortunato, A. Conti, K. R. Acharya

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26 Citations (SciVal)


Isolation, purification, amino acid sequence determination and X-ray crystal structure of buffalo α-lactalbumin were performed in order to gain further knowledge of the molecular basis of α-lactalbumin in the lactose synthase complex. The deduced amino acid sequence differs at one position from the bovine α-lactalbumin sequence (at position 17). The refined crystal structure at 2.3 Å is very similar to those previously reported for human and baboon α-lactalbumins. However, a portion of the molecule (residues 105-109) exhibits different conformation. It forms a 'flexible loop', and appears to be a functionally important region in forming the lactose synthase complex.

Original languageEnglish
Pages (from-to)91-95
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - 23 Sept 1996


  • Amino acid sequence
  • Buffalo milk
  • Crystal structure
  • α-Lactalbumin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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