Binding of 99mTc(113Sn)-MDP to human serum albumin. The influence of various technetium, tin, and MDP concentrations.
The HSA-binding of 99mTc incubated as 99mTc(113Sn)-MDP depends in vitro on the presence of competing anions normally present in plasma and on the MDP and Tc concentration, but is independent of the Sn concentration. The HSA-binding of 113Sn depends on the MDP and Sn concentration; not on the Tc concentration. 99mTc(Sn)-MDP binds to HSA as a unit. The binding of 99mTc(Sn)-MDP to plasma proteins in vivo is much lower as calculated from in vitro experiments because of competition between 99mTc(Sn)-MDP and endogenous anions for the same binding-sites.
D004164:Diphosphonates / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013667:Technetium / Q000494:pharmacology; D013669:Technetium Tc 99m Medronate / Q000097:blood*; D014001:Tin / Q000494:pharmacology
D004164:Diphosphonates; D012709:Serum Albumin; C023568:technetium Tc 99m (Sn)methylenediphosphonate; C027474:methylene diphosphonate; D013667:Technetium; D014001:Tin; D013669:Technetium Tc 99m Medronate