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The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.

biological chemistry hoppe-seyler

Microanalysis of the Amino-Acid Sequence of Monomeric β-Lactoglobulin I from Donkey ( Equus asinus ) milk. The Primary Structure and its Homology with a Superfamily of Hydrophobic Molecule Transporters