Investigations of the binding of 239Pu to liver cell membranes.
The binding of Pu to liver cell membranes was studied and compared with that of iron with which plutonium shares some physiological properties. The binding of both metals is sensitive to pH changes and they can be dissociated from their binding sites by chelating agents and transferrin. The metal-binding proteins can be extracted with detergents. Both metals have at least two binding sites, the molecular weights of which lie between 150 and 400 kDa; the isoelectric points for iron are 5.5 and 6.5, and for plutonium 6.0 and 6.5. The significance of these results for plutonium uptake into liver cells is discussed.
Planas-Bohne
F
F
Kernforschungszentrum Karlsruhe, Institut für Genetik and Toxikologie, F.R.G.
Kampmann
G
G
Olinger
H
H
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002712:Chlorides; D005290:Ferric Compounds / Q000378:metabolism; D007504:Iron Radioisotopes; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism; D009566:Nitrates; D011005:Plutonium / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D014168:Transferrin / Q000378:metabolism
D002712:Chlorides; D005290:Ferric Compounds; D007504:Iron Radioisotopes; D008565:Membrane Proteins; D009566:Nitrates; D014168:Transferrin; C015459:plutonium nitrate; D011005:Plutonium; C024555:ferric chloride