Development of an affinity chromatography resin for the purification of carcinogen binding proteins from mouse liver.

Pyrene, a structural analog of benzo[a]pyrene, is an effective competing ligand for high affinity carcinogen binding proteins in mouse liver. A pyrene-derivatized Sepharose gel was prepared for affinity chromatography purification of these proteins, and adsorbs all detectable [3H]B[a]P-binding activity from hepatic cytosol with the adsorption of less than 1% of total protein. Specific carcinogen binding activity is recovered from pyrene-derivatized Sepharose columns with the enrichment of a 33 kDa polypeptide. This chromatography resin represents a major step in the isolation of these unusual receptor-like binding proteins for aromatic hydrocarbon carcinogens.