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Partial Purification and Characterization of a Rat Liver Polychlorinated Biphenyl (PCB) Binding Protein.
Biochem. Pharmacol. 45, 885-891 (1993)
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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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
ISSN (print) / ISBN
0006-2952
e-ISSN
0006-2952
Zeitschrift
Biochemical Pharmacology
Quellenangaben
Band: 45,
Heft: 4,
Seiten: 885-891
Verlag
Elsevier
Begutachtungsstatus
Peer reviewed