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为探讨小牛心凝集素作为研究肿瘤细胞表面糖链的分子探针的可能性，以去唾液酸胎球蛋白－ＳｅｐｈａｒｏｓｅＣＬ－４Ｂ为亲和吸附剂，从小牛心组织中分离纯化了小牛心凝集素（ｃａｌｆｈｅａｒｔａｇｇｌｕｔｉｎｉｎ，ＣＨＡ），在不连续ＳＤＳ－ＰＡＧＥ上得到一条蛋白质带，分子量为１１．７ｋＤ。纯化的ＣＨＡ凝集新鲜兔红细胞的比活性提高了３６５倍，总活性回收率为８０．４％。糖抑制实验显示乳糖具有明显的抑制ＣＨＡ血凝活性作用，其产生抑制的最低浓度为０．６２５ｍｍｏｌ／Ｌ。此外，ＣＨＡ还可凝集人精子和Ｓ１８０肉瘤细胞，产生凝集的最低浓度分别为１０．５６ｍｇ／Ｌ和０．４７６ｍｇ／Ｌ。ＣＨＡ冻融后有蛋白质沉淀析出，凝血活性明显下降，但在４０～４３℃水浴中快速解冻后则血凝活性保持不变
In order to investigate the possibility of using calcein as a molecular probe to study the surface glycans of tumor cells, the calf heart was isolated and purified from the calf heart tissue using asialo-fetharose CL-4B as affinity adsorbent Lectin (calfheartagglutinin, CHA), obtained in the discontinuous SDS-PAGE a protein band, molecular weight of 11.7kD. The specific activity of purified CHA agglutinated fresh rabbit erythrocytes was increased by 365-fold and the total activity recovery was 80.4%. Sugar inhibition experiments showed that lactose has a significant inhibition of CHA hemagglutination activity, the minimum inhibitory concentration of 0.625mmol / L. In addition, CHA also agglutinated human spermatozoa and S180 sarcoma cells, producing the lowest concentrations of 10.56 mg / L and 0.476 mg / L, respectively. CHA freeze-thaw protein precipitation, coagulation activity decreased significantly, but in the 40 ~ 43 ℃ water bath after rapid thawing hemagglutination activity remained unchanged