The Complete Amino-Acid Sequence of Dimeric β-Lactoglobulin from Mouflon(Ovis ammon musimon)Milk
- 1 January 1987
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 368 (2) , 1313-1320
- https://doi.org/10.1515/bchm3.1987.368.2.1313
Abstract
.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.This publication has 20 references indexed in Scilit:
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