目的研究胆囊收缩素（ＣＣＫ）酪氨酸的硫酸化的意义及胚胎中ＣＣＫ结合蛋白的性质。方法用亲和层析法从鸡胚提取，纯化得到一种ＣＣＫ结合蛋白，经十二烷基硫酸钠聚丙烯酰胺凝胶电泳（ＳＤＳ－ＰＡＧＥ）达电泳纯。用辣根过氧化物酶标记的凝集素作点印迹法分析。结果其亚基Ｍｒ为３４×１０３，此结合蛋白与不同的ＣＣＫ－Ｓｅｐｈａｒｅｓｅ作用时显示，其与硫酸化的ＣＣＫ８、非硫酸化的ＣＣＫ８、硫酸化亮氨酸脑啡肽（Ｌｅｎ－Ｅｎｋ）结合活性较大，而与ＣＣＫ６、ＣＣＫ４、Ｌｅｕ－Ｅｎｋ结合活性较弱，且在ｐＨ６．５时结合最好。此结合蛋白与ＤＳＡ、ＷＧＡ、Ｓ－ＷＧＡ呈阳性反应，而不与ＣｏｎＡ、ＬＣＡ反应。结论ＣＣＫ羧基末端第７位上酪氨酸的硫酸化对ＣＣＫ结合活性有较大影响，且ＣＣＫ与其结合蛋白的结合呈ｐＨ依赖性。提示此结合蛋白含有糖链成分，以Ｎ－糖链为主，为多天线，呈平分型，不含核心岩藻糖。 Objective To study the significance of the sulfation of cholecystokinin (CCK) tyrosine and the properties of CCK-binding proteins in embryos. Methods The CCK-binding protein was extracted from chick embryo by affinity chromatography and purified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Horseradish peroxidase-labeled lectin was analyzed by dot blotting. As a result, its subunit Mr was 34x103. The binding of this binding protein to different CCK-Sepharese showed that it binds to sulfated CCK8, non-sulfated CCK8, and Len-Enk The activity of CCK6, CCK4 and Leu-Enk is relatively weak, and the binding activity is best at pH 6.5. The binding protein and DSA, WGA, S-WGA positive reaction, but not with ConA, LCA reaction. Conclusions The sulfation of tyrosine on the 7th carboxyl terminus of CCK has a significant effect on the CCK binding activity, and the binding of CCK to its binding protein is pH-dependent. Tip of this binding protein containing sugar chain components to N-sugar chain-based, multi-antenna, was a flat type, free of core fucose.