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We describe a two-step method that uses wheat germ agglutinin immobilized
on Sepharose gel followed by immunoaffinity chromatography (IAC) to extract
recombinant human erythropoietin and Darbepoetin from equine plasma. Lectin
affinity chromatography was shown to be an effective approach for isolating
these epoetins from plasma and in combination with IAC; this method gave
superior recovery when compared to the use of the latter technique alone.
Moreover, due to the ease with which it can be scaled up, it is particularly
well suited for pre-concentrating larger volumes of samples prior to IAC and
this provides a facile way of improving the overall sensitivity with which
these foreign proteins can be detected in equine plasma.