Covalent binding of DBCP to proteins in vitro

[¹⁴C] 1,2-Dibromo-3-chloropropane (DBCP) was incubated with rat liver 9000 × g supernatant in order to investigate the covalent binding of DBCP to proteins. Radioactivity incorporated into proteins was dependent on the microsomal oxidase system, but was not prevented by sufficient puromycin to inhibit protein synthesis. From these results DBCP was considered to bind to proteins covalently after activation by microsomal oxidase.