The binding of 99mTc(Sn)-MDP complexes to human serum albumin and other blood proteins determined with gel chromatography and ultrafiltration.

The binding of 99mTc(Sn)-MDP to human serum albumin and other blood proteins was investigated by gel chromatography and ultrafiltration. During gel chromatography dissociation of the 99mTc(Sn)-MDP-protein complex occurs: thus, it is not a suitable technique for the determination of protein binding. The values found with ultrafiltration have to be corrected for non-ultrafiltrable TcO2.

Anion exchange chromatography of 99mTc(Sn)-MDP complexes: influence of eluent composition, determination of void volume and charge of the main component.

99mTc(Sn)-MDP complexes have been prepared by reduction of 99mTcO4- by Sn(II) in the presence of MDP. These complexes were separated on an anion exchange column. The necessity of the addition of the ligand and the reducing agent to the eluent to avoid decomposition during chromatography is demonstrated.

The influence of Sn(IV) on the mean size of 99mTc(Sn)MDP constituents at neutral pH.

The effect of addition of Sn(IV), Mg(II) and Ca(II) on the mean size of the 99mTc-containing constituents of a 99mTc(Sn)MDP reaction mixture was determined by a gel chromatographic batch procedure that does not disturb the equilibria in the mixture.