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)

International Journal of Nuclear Medicine and Biology
J DuffieldS A Proctor

Abstract

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.

Citations

Jun 28, 2011·Nature Chemical Biology·Mark P JensenL Soderholm
Jul 7, 2015·Advanced Drug Delivery Reviews·Elias FattalGuillaume Phan
Jul 26, 2011·Biochimica Et Biophysica Acta·John B Vincent, Sharifa Love
May 23, 2014·International Journal of Radiation Biology·Manuel KastlMaria Antonia Lopez
Dec 2, 2009·Chemistry : a European Journal·Aurélie JeansonChristophe Den Auwer
Jan 26, 2020·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Lokpati MishraTusar Bandyopadhyay
Nov 13, 2003·Chemical Reviews·Anne E V GordenPatricia Durbin
Aug 1, 1986·Journal of Inorganic Biochemistry·G M ThenW G Thies

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