Jiang M
PUMC Hospital, Beijing.
Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 1993 Apr;15(2):138-42.
By using the partially purified recombinant human erythropoietin (rHuEPO) as an antigen, two hybridoma clones have been obtained that secrete monoclonal antibodies against human erythropoietin. Intrasplenic immunization was successfully used in this experiment. The prepared monoclonal antibodies showed high specificity to human EPO by Ouchterlony, ELISA, dot blot and Western blot tests. They were also found to inhibit the biological activity of rHuEPO in a concentration-dependent manner by an in vitro bioassay. In the future, these monoclonal antibodies will be used as the solid phase antibodies in an enzyme-linked immunosorbent assay and as a probe for the purification of native erythropoietin and for the further studies of the hormone and its mechanism of action.