RADIOLABELING ANTIBODIES WITH HO-166

We report the preliminary results from radiolabeling of a chelate-conj ugated antibody with Ho-166 produced from the beta(-)-decay of Dy-166. Ho-166 was separated from mg quantities of Dy target by reverse phase ion-exchange chromatography employing a cation exchange HPLC column a nd 0.085 M alpha-HIBA at pH = 4.3 as eluent. Evaporation to dryness of Ho-166 fraction (up to 25 mL) and thermal decomposition of alpha-HIBA yielded Ho-166 in a dry state which was then solubilized in 0.5 mL of 0.1 M HCl. Subsequent radiolabeling of CHX-B-DTPA conjugated 135-14 m onoclonal antibodies with purified Ho-166 was readily achieved with si milar to 80% efficiency and with a specific activity of 3-4 mCi of Ho- 166 per mg of protein. Ho-166-antibody conjugates are stable with rega rds to transferrin challenge for a period of 50 h. Further, it was sho wn that any Fe3+ ions present in alpha-HIBA as an impurity interfere w ith the labeling. (C) 1997 Elsevier Science Ltd.