来自摩弗伦羊（欧洲盘羊摩弗伦亚种）奶的二聚体β-乳球蛋白的完整氨基酸序列。
The complete amino-acid sequence of dimeric beta-lactoglobulin from mouflon (Ovis ammon musimon) milk.
作者信息
Godovac-Zimmermann J, Conti A, Napolitano L
机构信息
Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra City A.C.T.
出版信息
Biol Chem Hoppe Seyler. 1987 Oct;368(10):1313-9. doi: 10.1515/bchm3.1987.368.2.1313.
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.
已从摩弗伦羊（欧洲盘羊摩弗伦亚种）奶中分离出β-乳球蛋白，并确定了其完整的一级结构。该蛋白质以二聚体形式分离得到，分子量为37 kDa。通过对天然蛋白质进行微量测序确定了氨基酸序列，胰蛋白酶切割后得到了肽段。胰蛋白酶肽段通过反相高效液相色谱法进行分离。摩弗伦羊β-乳球蛋白的一级结构与反刍动物β-乳球蛋白显示出密切的相似性。第20位存在组氨酸表明该蛋白质属于二聚体绵羊β-乳球蛋白的B型。摩弗伦羊β-乳球蛋白是一条由162个氨基酸组成的多肽链，含有两个二硫键和一个游离巯基。文中讨论了其与胆汁素结合蛋白、嗅觉上皮的BG蛋白和视黄醇结合蛋白的结构相似性。
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