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Enzymic Studies of Bile Acid Metabolism

I. 6-HYDROXYLATION OF CHENODEOXYCHOLIC AND TAUROCHENODEOXYCHOLIC ACIDS BY MICROSOMAL PREPARATIONS OF RAT LIVER

From the ¹ From the Departments of Biochemistry and Dermatology, University of Miami School of Medicine, Miami, Florida 33136

6ß-Hydroxylation of chenodeoxycholic acid-24-¹⁴C and taurochenodeoxycholic acid-24-¹⁴C was demonstrated in vitro by cell-free preparations of rat liver. The enzymic activity, requiring O₂ and NADPH, was located in the microsomes prepared in 0.1 m phosphate buffer and could be stimulated by addition of the 105,000 x g supernatant fluid.

The microsomal fraction prepared in 0.01 m phosphate buffer had full activity and was not further stimulated by the 105,000 x g supernatant fluid. A clear extract made by suspending this microsomal pellet in 1.0 m phosphate and subsequently centrifuging it at 105,000 x g contained the complete 6ß-hydroxylase system. The activity of the 1.0 m phosphate extract was inhibited by sulfhydryl reagents, Cu⁺⁺, cytochrome c, and CO. The inhibition by CO could be reversed by light. The presence of cytochrome b₅ and the CO-binding pigment, P-450, in the extract was detected by differential spectrophotometry.

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