Effects of added protein (bovine serum albumin) on the rate and enantiotopic selectivity of oxidative O-demethylation of methoxychlor in rat liver microsomes

The addition of bovine serum albumin (BSA) to rat liver microsomal suspensions during the O-demethylation of methoxychlor (1,1-bis(4-methoxyphenyl)-2,2,2-trichloroethane) produced a good substrate concentration-reaction rate relationship, and allowed us to determine the rate parameters for this reaction. The apparent K_m became larger when the albumin content was increased, whereas V_max was not changed. The enantiotopic selectivity of the reaction dramatically changed when the substrate concentration was increased in the absence of BSA in phenobarbital-treated rat liver microsomes.