Abstract
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 language | English |
---|---|
Pages (from-to) | 91-95 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 394 |
Issue number | 1 |
DOIs | |
Publication status | Published - 23 Sept 1996 |
Keywords
- Amino acid sequence
- Buffalo milk
- Crystal structure
- α-Lactalbumin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology