在大肠杆菌中表达了一种抗肿瘤转移多肽——人纤连蛋白（ＦＮ） 的ＣｅｌｌＩ－Ｈｅｐ Ⅱ－ＣｅｌｌⅡ三结构域重组多肽（ＣＨ８２）， 表达效率达２１％ 。在低温 （２２ ℃） 培养表达时， ＣＨ８２大部分为可溶性产物， 经ＤＥＡＥ－５２ 层析及Ｈｅｐａｒｉｎ－ａｇａｒｏｓｅ亲和层析可得到纯品； 在高温（３７ ℃） 培养表达时， ＣＨ８２ 主要以包涵体形式出现， 经尿素变性与复性处理后，可通过Ｈｅｐａｒｉｎ－ａｇａｒｏｓｅ 亲和层析得到纯品。所得纯品均具有结合肝素和结合细胞的功能， 且结合细胞的能力比双结构域ＦＮ更强， 表明两个结合细胞的功能结构域均有活性 A recombinant CellI-Hep Ⅱ-CellⅡ recombinant polypeptide (CH82) was expressed in Escherichia coli which expressed anti-tumor metastatic peptide - human fibronectin (FN). The efficiency of expression was 21%. Most of CH82 was soluble when cultured in low temperature (22 ℃), and purified by DEAE-52 and Heparin-agarose affinity chromatography. When cultured in high temperature (37 ℃), CH82 mainly contained Body form, after urea denaturation and renaturation treatment, can be purified by Heparin-agarose affinity chromatography. The resulting pure product has the function of binding heparin and bound cells, and the capacity of binding to cells is stronger than that of double-domain FN, indicating that both of the functional domains of bound cells are active