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Isolation and characterization of two antigenically active peptides from bovine β-lactoglobulin-A

机译:牛β-乳球蛋白-A中两种抗原活性肽的分离与鉴定

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摘要

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.
机译:牛β-乳球蛋白-A用胰蛋白酶水解,产生的肽混合物不会与抗天然蛋白质的兔抗体一起沉淀,但仍会抑制抗原-抗体反应。通过离子交换色谱法分离水解产物,发现其包含七个抗原活性部分。发现这些级分中的两个是均质肽。在豚鼠的血凝,絮凝和被动性皮肤过敏反应中,每种都抑制抗原与针对完整蛋白的抗体的反应。一种肽的分子量为950,另一种肽的分子量为575。两种肽均包含大约相等数量的极性和非极性氨基酸。

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