In vitro evidence for CCl4 metabolites covalently bound to lipoprotein micelles.
CCl4-induced impairment of the lipoprotein secretion pathway of intact rat hepatocytes was carried out using 14CCl4 to check the possibility of binding to lipoproteins by CCl4 metabolites. After separation of different cell suspension fractions by means of ultracentrifugation and chemical precipitation procedures, a significant amount of the radioisotope was found covalently bound to the lipid and protein components of low density lipoproteins. Suitable experiments demonstrated that the bound radioisotope was represented by CCl4 metabolites and not by unactivated CCl4.
D000818:Animals; D002250:Carbon Radioisotopes; D002251:Carbon Tetrachloride / Q000378:metabolism*; D003102:Colloids; D008074:Lipoproteins / Q000378:metabolism*; D008077:Lipoproteins, LDL / Q000302:isolation & purification / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D008297:Male; D008823:Micelles; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains
D002250:Carbon Radioisotopes; D003102:Colloids; D008074:Lipoproteins; D008077:Lipoproteins, LDL; D008823:Micelles; D002251:Carbon Tetrachloride