TY - JOUR
T1 - Radiolabeling antibodies with holmium-166
AU - Dadachova, Ekaterina
AU - Mirzadeh, Saed
AU - Smith, Suzanne V.
AU - Knapp, F. F.
AU - Hetherington, Eric L.
N1 - Funding Information:
Acknowledgements--The authors acknowledge Professor G. J. Beyer, Division of Nuclear Medicine, HCU Geneva, Switzerland for valuable discussions. Research at ORNL was supported by the Office of Health and Environmental Research, U.S. Department of Energy under contract DE-AC05-960R22464 with Lockheed Martin Energy Research Corporation. Research at ANSTO was supported by the Commonwealth of Australia.
PY - 1997/4
Y1 - 1997/4
N2 - We report the preliminary results from radiolabeling of a chelate-conjugated antibody with 166Ho produced from the β--decay of 166Dy. Ho-166 was separated from mg quantities of Dy target by reverse phase ion-exchange chromatography employing a cation exchange HPLC column and 0.085 M α-HIBA at pH = 4.3 as eluent. Evaporation to dryness of 166Ho fraction (upto 25 mL) and thermal decomposition of α-HIBA yielded 166Ho 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 monoclonal antibodies with purifled 166Ho was readily achieved with ~80% efficiency and with a specific activity of 3-4 mCi of 166Ho per mg of protein. 166Ho-antibody conjugates are stable with regards to transferrin challenge for a period of 50 h. Further, it was shown that any Fe3+ ions present in α-HIBA as an impurity interfere with the labeling.
AB - We report the preliminary results from radiolabeling of a chelate-conjugated antibody with 166Ho produced from the β--decay of 166Dy. Ho-166 was separated from mg quantities of Dy target by reverse phase ion-exchange chromatography employing a cation exchange HPLC column and 0.085 M α-HIBA at pH = 4.3 as eluent. Evaporation to dryness of 166Ho fraction (upto 25 mL) and thermal decomposition of α-HIBA yielded 166Ho 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 monoclonal antibodies with purifled 166Ho was readily achieved with ~80% efficiency and with a specific activity of 3-4 mCi of 166Ho per mg of protein. 166Ho-antibody conjugates are stable with regards to transferrin challenge for a period of 50 h. Further, it was shown that any Fe3+ ions present in α-HIBA as an impurity interfere with the labeling.
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U2 - 10.1016/S0969-8043(96)00269-2
DO - 10.1016/S0969-8043(96)00269-2
M3 - Article
C2 - 9106989
AN - SCOPUS:0031127085
SN - 0969-8043
VL - 48
SP - 477
EP - 481
JO - Applied Radiation and Isotopes
JF - Applied Radiation and Isotopes
IS - 4
ER -