从牛β-乳球蛋白A中分离并鉴定两种具有抗原活性的肽段。
Isolation and characterization of two antigenically active peptides from bovine beta-lactoglobulin-A.
作者信息
Bing D H, Stavitsky A B
出版信息
Immunology. 1968 Aug;15(2):305-17.
Bovine β-lactoglobulin-A was hydrolysed with trypsin to yield a mixture of peptides which would not precipitate with rabbit antibody against the native protein, but would still inhibit the antigen—antibody reaction. The hydrolysate was fractionated by ion exchange chromatography and found to contain seven antigenically active fractions. Two of these fractions were found to be homogeneous peptides. Each inhibited the reaction of antigen with antibody against the intact protein in haemagglutination, flocculation and passive cutaneous anaphylaxis reaction in guinea-pigs. One of the peptides had a molecular weight of 950 and the other had a molecular weight of 575. Both contained about equal numbers of polar and apolar amino acids.
用胰蛋白酶水解牛β-乳球蛋白-A，得到一种肽混合物，该混合物不会与抗天然蛋白质的兔抗体沉淀，但仍能抑制抗原-抗体反应。通过离子交换色谱法对水解产物进行分离，发现其含有七个具有抗原活性的组分。其中两个组分是均一的肽。在豚鼠的血凝、絮凝和被动皮肤过敏反应中，每一种都能抑制抗原与抗完整蛋白质抗体的反应。其中一种肽的分子量为950，另一种为575。两者所含极性和非极性氨基酸数量大致相等。
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