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Isolation and characterization of conformation sensitive antierythropoietin
monoclonal antibodies: effect of disulfide bonds and carbohydrate on
recombinant human erythropoietin structure
S Elliott, D Chang, E Delorme, C Dunn, J Egrie, J Giffin, T Lorenzini, C Talbot and L Hesterberg
Amgen Inc, Thousand Oaks, CA 92320, USA.
We have isolated and characterized three anti-recombinant human
erythropoietin (rHuEPO) monoclonal antibodies (MoAbs) that recognize
nonoverlapping epitopes on rHuEPO. Anti-EPO MoAb D11 neutralizes rHuEPO
activity whereas MoAbs F12 and 9G8A do not. This suggests that D11 may bind
to the rHuEPO active site. MoAbs F12 and D11 recognize conformation
dependent epitopes whereas 9G8A does not. Immunoassays were developed for
each monoclonal. The 9G8A immunoassay was novel and useful because
immunoreactivity increased when rHuEPO was denatured. Disruption of
disulfide bonds or removal of carbohydrate increased 9G8A immunoreactivity,
which suggests that these elements are important for rHuEPO structure or
stability.
Volume 87,
Issue 7,
pp. 2714-2722,
04/01/1996
Copyright © 1996 by The American Society of Hematology
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