CHO-EPO C2 cells were cultured in the Packed Bed Bioreactor with free-fetal bovine serum medium, and the supertant contained 2 000～3 000 U/ml of recombinant Human EPO(rHuEPO). The SDS-PAGE result of the final products from the reported purification schemes was a single band, which purity was over 98% with measurement of UV scanning. The specific activity was 1.5×10⁵ U/mg protein. Reserch showed that the molecular weight was about 35～40 ku and the pI was about 3.75～4.15.The product possessed the antigenity of native HuEPO. The peptide electrophoresis result was in accord with theory deducation. 15 amino acid sequence of rHuEPO N terminal was as the same as native HuEPO. All these results described above revealed that the final product were high purity rHuEPO and the purification procedure was rapid and efficient, which can be used to produce clinic rHuEPO in large scale.