【摘要】 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．更多还原

【Abstract】 The casein phosphopeptides(CPP) obtained by pancreatic hydyolysis was purified by anion exchange resin, and then was further separated into two fractions after gel filtration. From the main fraction containing 85% of the total CPP, four major components were purified by two runs of HPLC on C 18 reverse phase column. The amino acid composition and the sequence of the N terminal of each component were analyzed respectively by an amino acid analyzer and a protein sequencer. Among the four components, three were identified respectively as αs1(61～79),αs1(43～79) and β(7～24). The peptide chains of pancreatic CPP were found to be shorter than that of tryptic CPP.更多还原