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Partial purification and characterization of a rat liver polychlorinated biphenyl (PCB) binding protein.

Biochem. Pharmacol. 45, 885-891 (1993)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
A protein capable of specifically binding polychlorinated biphenyls (PCB) was partially purified from rat liver cytosol. After labeling with [3H]2,2',4,4',5,5'-hexachlorobiphenyl (6-CB), protein enrichment was guided by monitoring the protein-bound radioactivity through a sequence of purification steps including ion exchange chromatography and preparative gel electrophoresis. In addition, specific binding tests of individual fractions were carried out. An average 100-fold enrichment of the 40 kDa protein was achieved. A variety of ligands were tested in competitive binding studies with 6-CB. Whereas penta- and hexachloro-PCB congeners are high affinity competitors, the 3,3',4,4'-tetrachlorobiphenyl congener does not compete for 6-CB binding. Studies on the species and tissue distribution suggest a prevalence of the binding protein in tissues of the rat. Since the natural physiological ligand of the protein has not yet been identified, the function of the protein can only be speculated on.
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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 0006-2952
e-ISSN 0006-2952
Quellenangaben Volume: 45, Issue: 4, Pages: 885-891 Article Number: , Supplement: ,
Publisher Elsevier
Reviewing status Peer reviewed