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- Title
The Complete Amino-Acid Sequence of Dimeric β-Lactoglobulin from Mouflon (O vis ammon musimon) Milk.
- Authors
GODOVAC-ZIMMERMANN, Jasminka; CONTI, Amedeo; NAPOLITANO, Lorenzo
- Abstract
β-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 β-lactoglobulin shows close similarity to ruminant β-lactoglobulins. The presence of His at position 20 indicates that this protein belongs to the B-type of dimeric ovine β-lactoglobulins. Mouflon β-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.
- Publication
Biological Chemistry, 1987, Vol 368, Issue 2, p1313
- ISSN
1431-6730
- Publication type
Article