The complete amino-acid sequence of dimeric beta-lactoglobulin from mouflon (Ovis ammon musimon) milk.
beta-Lactoglobulin from Mouflon (Ovis ammon musimon) milk has been isolated and its complete primary structure determined. This protein has been isolated in dimeric form and has a molecular mass of 37 kDa. The amino-acid sequence has been determined by microsequencing of the native protein and the peptides were obtained after tryptic cleavage. The tryptic peptides were isolated by reversed phase high-performance liquid chromatography. The primary structure of mouflon beta-lactoglobulin shows close similarity to ruminant beta-lactoglobulins. The presence of His at position 20 indicates that this protein belongs to the B-type of dimeric ovine beta-lactoglobulins. Mouflon beta-lactoglobulin is a 162 amino acid long polypeptide chain with two disulphide bridges and one free thiol group. Structural similarities to the bilin-binding protein, BG protein from olfactory epithelium and retinol-binding protein are discussed.
Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra City A.C.T.
J
J
Godovac-Zimmermann
A
A
Conti
L
L
Napolitano
D000595:Amino Acid Sequence; D000818:Animals; D001053:Apolipoproteins / Q000032:analysis; D053399:Apolipoproteins D; D004847:Epithelial Cells; D004848:Epithelium / Q000032:analysis; D005260:Female; D006868:Hydrolysis; D007782:Lactoglobulins / Q000032:analysis*; D008969:Molecular Sequence Data; D012756:Sheep; D014357:Trypsin
D001053:Apolipoproteins; D053399:Apolipoproteins D; D007782:Lactoglobulins; D014357:Trypsin