中文摘要：

目的研究利用固相金属亲和层析纯化重组类人胶原蛋白的洗脱方法,以优化分离纯化的条件。方法将吸附了重组类人胶原蛋白的层析柱采用降低pH,增大离子强度和增大NH_4Cl浓度3种方法进行洗脱。结果采用增大NH4Cl浓度的方法进行洗脱所得的洗脱峰面积最大,洗脱体积最小,纯化后重组类人胶原蛋白的纯度达97.9%,回收率为68.6%,纯化倍数为2.78。结论采用固相金属亲和层析纯化重组类人胶原蛋白是可行的,可有效地对重组类人胶原蛋白进行纯化。

英文摘要：

Aim To choose the best conditions of immobilized metal affinity chromatography （IMAC） for separation of the recombinant human-like collagen. Methods The column which had adsorbed the recombinant human-like collagen was eluted by three methods. Method one was to reduce pH. Mehtod two was to aggrandize ionic strength. Method three was to aggrandize the NH4Cl concentration. Results The eluting peak area of method three was the biggest, and the eluting volume was the least. The purity of recombinant human-like collagen could be 97. 9%, recovery was 68.6%, purification fold was 2. 78. Conclusion The best eluting method was the gradient elution by aggrandizing the NHaCI concentration. Recombinant human-like collagen could be effectively purified by this method.