Amino acid sequence and crystal structure of buffalo α‐lactalbumin

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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.

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