Microanalysis of the amino-acid sequence of monomeric beta-lactoglobulin I from donkey (Equus asinus) milk. The primary structure and its homology with a superfamily of hydrophobic molecule transporters.
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.
Godovac-Zimmermann
J
J
Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra.
Conti
A
A
James
L
L
Napolitano
L
L
D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D006736:Horses / Q000235:genetics*; D007782:Lactoglobulins / Q000235:genetics* / Q000302:isolation & purification; D008832:Microchemistry; D008892:Milk; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D012177:Retinol-Binding Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D007782:Lactoglobulins; D010446:Peptide Fragments; D012177:Retinol-Binding Proteins