The binding of plutonium to transferrin in the presence of tri-n-butyl phosphate or nitrate and its release by diethylenetriaminepenta-acetate and the tetrameric catechoylamide ligand LICAMC(C).
The binding of plutonium to human apo-transferrin and to rat serum was investigated following delivery of the metal to the protein either as the plutonium-tri-n-butyl phosphate (Pu-TBP) complex in n-dodecane or as plutonium nitrate. Chromatographic behaviour, the failure to bind to iron-saturated transferrin and the release of plutonium by the chelating agents CaNa3DTPA and 3,4,3-LICAM(C) suggest that the transferrin complexes formed from the two plutonium compounds are similar. The tetracatechoylamide ligand LICAM(C) was found to be about 500 times more effective than DTPA, on a molar basis, for the release of plutonium from transferrin in rat serum.
D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D009566:Nitrates / Q000097:blood; D010755:Organophosphates / Q000097:blood; D004369:Pentetic Acid / Q000494:pharmacology; D011005:Plutonium / Q000097:blood*; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D013095:Spermidine / Q000031:analogs & derivatives / Q000494:pharmacology; D014168:Transferrin / Q000378:metabolism*
D002614:Chelating Agents; D009566:Nitrates; D010755:Organophosphates; D014168:Transferrin; D011005:Plutonium; C034834:LICAM-C; D004369:Pentetic Acid; C009524:tributyl phosphate; D013095:Spermidine