人胎儿血红蛋白的纯化及免疫活性鉴定

目的研究胎儿血红蛋白纯化的最佳方法，并对其进行免疫活性鉴定。方法采用生理盐水洗涤、四氯化碳萃取得到粗提胎儿血红蛋白，再经sephadexG50凝胶层析柱纯化。纯化后的胎儿血红蛋白利用SDS—PAGE电泳、蛋白质印迹鉴定其性质。结果获得了具有生物活性的胎儿血红蛋白．经SDS-PAGE电泳鉴定纯化蛋白杂带消失，蛋白单体相对分子质量为16000Mr，纯度为95％，蛋白质印迹结果显示纯化后的蛋白具有良好的抗原性。结论该方法成功获得了纯度较高的胎儿血红蛋白，且操作简便，纯化效果好。

Studies on Purification and Immunocompetence Characterization of Fetal Hemoglobin

Objective To study the optimal condition for the purification of fetal hemoglobin （HbF）. Method The pykno-fetal hemoglobin was eluted by isotonic Na chloride（NS） and extracted by tetrachloride （CC14）. After the above processes, the product was purified by sephadexG50 gel chromatography. The purity of the isolated HbF was identified by SDS-PAGE, Western Blot analysis. Results The SDS-PAGE analysis showed that the protein purified by sephadexG50 gel chromatography removed hybridprotein and manifested biological activity with relative molecularmass of 16000. Its purity could reach about 95%. Conclusion HbF with high-purity from the foetal blood can be obtained by our method and the procedure employed in this experiment is easy to handle and the purification efficiency is ideal.