A methylsulfonyl metabolite of a polychlorinated biphenyl can serve as a ligand for liver fatty acid binding protein in rat intestinal mucosa.

When a 100,000 x g supernatant from rat intestinal mucosa was incubated with 4,4'-bis([3H]methylsulfonyl)-2,2',5,5'-tetrachlorobiphenyl, [(CT3SO2)2TCB] a (CT3SO2)2TCB-protein complex was formed. The (CT3SO2)2TCB-protein complex was isolated and purified using gel filtration and ion-exchange chromatography. The protein portion of this complex was characterized to be liver fatty acid binding protein (L-FABP) by SDS-polyacrylamide gel electrophoresis and immunoblot analysis. No cross reactivity was observed in the immunoblot analysis between the purified protein and anti-heart or anti-intestinal fatty acid binding protein. (CT3SO2)2TCB was extractable from L-FABP and therefore not covalently bound to L-FABP.