Partial saturation of rat liver Cd-binding proteins by Cd2+ in vivo.
Liver Cd-binding proteins (Cd-BP) were isolated from rats chronically treated with 109Cd-labeled CdCl2 for ten days. Fractions purified using Sephadex G-75 and DEAE-Sephadex were characterized and found to be similar to those isolated by other investigators. Cd-binding was not saturated in any of the preparations and significant amounts of Cu and Zn were also found bound to the proteins. The percentage of saturation of Cd-BP1, and Cd-BP2 was independently determined by atomic absorption spectrometry and spectroscopy at 254 nm. These results indicate that the fraction of binding sites unoccupied by Cd on Cd-BP approaches 20% in vivo.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002104:Cadmium / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D003300:Copper / Q000032:analysis; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008670:Metals / Q000032:analysis; D008722:Methods; D008970:Molecular Weight; D011485:Protein Binding; D011868:Radioisotopes; D051381:Rats; D013054:Spectrophotometry, Atomic; D015032:Zinc / Q000032:analysis / Q000494:pharmacology
D000596:Amino Acids; D002352:Carrier Proteins; D008670:Metals; D011868:Radioisotopes; D002104:Cadmium; D003300:Copper; D015032:Zinc