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将离子交换色谱、凝胶过滤色谱、高压液相色谱及毛细管色谱等分离纯化技术结合使用，从酪蛋白磷酸肽（ＣＰＰ）制品中分离出３ 个纯组分，并对各组分的氨基酸组成和Ｎ 末端２～３ 个氨基酸序列进行了分析测定，从而确定了３ 个组分的结构，它们分别是αｓ１（６１～７９）、αｓ１（４３～７９）和β（７～２４）．与用胰蛋白酶水解酪蛋白得到的ＣＰＰ比较，用胰酶水解得到的ＣＰＰ肽链较短．
Three pure components were isolated from casein phosphopeptide (CPP) by ion exchange chromatography, gel filtration chromatography, high pressure liquid chromatography and capillary chromatography. The amino acid composition of each component And the N-terminal 2 to 3 amino acid sequences were analyzed and determined to determine the structure of the three components, which are αs1 (61 ~ 79), αs1 (43 ~ 79) and β (7 ~ 24). The CPP peptide chains obtained by trypsin hydrolysis were shorter than those obtained by trypticase casein hydrolysis.