PMID: 3320770Jan 1, 1987Paper

Inducible high-affinity binding site for benzo(a)pyrene in cytosol from rat liver

Neoplasma
Z MureşanN Voiculetz

Abstract

By the use of the dextran-coated charcoal method the presence of a high-affinity binding site for benzo(a)pyrene in the cytosol from rat liver (R strain) has been demonstrated. This binder was saturable by ligand concentration and by time. Sucrose density gradient analysis after charcoal treatment revealed one major peak of radioactivity sedimenting at 4.4 S which was displaceable by a 100-fold molar excess of nonlabeled benzo(a)pyrene. Benzo(a)pyrene binding to liver cytosol was sensitive to protease treatment of the cytosol suggesting that the binder was a protein. Saturation and Scatchard plot analysis of benzo(a)pyrene binding indicated a high-affinity (Kd = 4.7 nmol) and a relatively low binding capacity (Bmax = 379 fmol/mg cytosolic protein), allowing, to denote this binder as a receptor for benzo(a)pyrene. Competition studies showed that this cytosolic receptor was distinct from steroid hormone receptors since benzo(a)pyrene binding was partially inhibited by aromatic carcinogens 3-methylcholanthrene and benz(a)anthracene but not by estradiol, progesterone or cortisol. R strain rats used in these experiments were sensitive to induction with 3-methylcholanthrene which produced the increase of cytochrome Pl-450 content in ...Continue Reading

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