High Expression, Purification, Quality Control of rhEPO-Fc Fusion Protein
rhEPO-Fc融合蛋白的表达、纯化及质量研究

To explore the technics for high expression, purification, quality control of recombinant human erythropoietin and IgG Fc fusion protein, rhEPO-Fc fusion protein expressed by CHO cells in serum-free medium was collected and purified with a three-step purification process-affinity chromatography, ion exchange chromatography and molecular sieve chromatography; and its quality was controlled by protein concentration, SDS-PAGE,Western-blot,HPLC,ELISA and IEF, et al. The research findings are that the expression output of rhEPO-Fc was highly reached 2g/L, the purify rate was over 45%, its purify was over 98%, its relative molecular weight is about 60kDa, t1/2 in vivo of rhEPO-Fc is over 38h, western blot analysis showed rhEPO-Fc has nature antigenicity. The expression output and purify rate of the produce technics is high, quality inspection methods are stability and reliable, which could be fit for in large-scale production of rhEPO-Fc.