Abstract

Significant amounts of cytochrome P-450 have been detected spectrally in purified nucleoli obtained from the livers of 3-methylcholanthrene-treated rats. Using monospecific antibody to microsomal cytochrome P-450_c (P-448), we have shown that the nucleolar and microsomal enzymes are immunochemically identical. These nucleoli also contained epoxide hydrolase and NADPH-cytochrome c reductase activities, both of which were immunochemically identical to their respective microsomal counterparts.