title: 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.
abstract: 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.
authors: Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra.
authors: J
authors: J
authors: Godovac-Zimmermann
authors: A
authors: A
authors: Conti
authors: L
authors: L
authors: James
authors: L
authors: L
authors: Napolitano
mesh_terms: 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
chemical_list: D007782:Lactoglobulins; D010446:Peptide Fragments; D012177:Retinol-Binding Proteins