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Buff, K. ; Bründl, A.

Specific binding of polychlorinated biphenyls to rat liver cytosol protein.

Biochem. Pharmacol. 43, 965-970 (1992)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
Specific binding of polychlorinated biphenyls (PCBs) to rat liver cytosol protein has been detected using the 3H-labeled PCB probe 2,2',4,4',5,5'-hexachlorobiphenyl (6-CB). Binding of 6-CB to cytosol protein is displaced by its non-radioactive congener, is of high affinity (K(d) ~ 3nM) and is saturable (maximal binding capacity B(max) ~ 600 pmol/mg protein). 6-CB binding is not found in liver cytosol of animals fed a PCB-supplemented diet (500 ppm PCB for 5 days). Binding is also in vitro inhibited by high concentrations of triglyceride. PCB congeners such as 3,3',4,4',5-pentachlorobiphenyl as well as the thyroid hormones 3,5,3',5'-tetraiodothyronine and 3,5,3'-triiodothyronine (the latter hormone with an order of magnitude lower affinity) compete for the PCB binding site. On the other hand, a number of biochemically important compounds including the PCB core compound biphenyl and the hormone ligands dexamethasone and estradiol, as well as 2,3,7,8-tetrachlorodibenzo-p-dioxin, do not compete for the 6-CB binding site. The data provide the first evidence of specific binding of unmetabolized PCB congeners to distinct binding sites in rat liver cytosol.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
ISSN (print) / ISBN 0006-2952
e-ISSN 0006-2952
Journal Biochemical Pharmacology
Quellenangaben Volume: 43, Issue: 5, Pages: 965-970 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Molecular Toxicology and Pharmacology (TOX)