Hybridomas for production of monoclonal antibodies to human erythropoietin
S Yanagawa, S Yokoyama, K Hirade, R Sasaki, H Chiba, M Ueda and M Goto
Human urinary erythropoietin has been highly purified by a combination of
conventional purification methods and immunoadsorbent columns packed with
hybridoma-produced antibodies against contaminants that seemed difficult to
separate from erythropoietin by the usual means. By using the partially
purified erythropoietin as an antigen, three hybridoma clones have been
obtained that secrete monoclonal antibodies against erythropoietin. One of
the clones has been quite stable, with a rapid growth rate and high
production of antibody. Western blotting technique with monoclonal
antibodies revealed occurrence of two species of erythropoietin. The
monoclonal antibody will be useful as a probe for the purification of
erythropoietin and for further studies of the hormone and its mechanism of
action.
Volume 64,
Issue 2,
pp. 357-364,
08/01/1984
Copyright © 1984 by The American Society of Hematology
