Journal of Lipid Research (Oct 1988)

Characterization of 6 alpha-hydroxylation of taurochenodeoxycholic acid in pig liver.

  • H Boström

DOI
https://doi.org/10.1016/s0022-2275(20)38784-8
Journal volume & issue
Vol. 27, no. 8
pp. 807 – 812

Abstract

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The properties of the species-specific 6 alpha-hydroxylation of taurochenodeoxycholic acid were studied in subcellular fractions from pig liver. The hydroxylation was observed in microsomes but not in mitochondria. A partially purified cytochrome P-450 fraction in the presence of NADPH-cytochrome P-450 reductase, NADPH, and phospholipid catalyzed 6 alpha-hydroxylation of taurochenodeoxycholic acid at a 160-fold higher rate than the microsomes. This cytochrome P-450 fraction did not catalyze 6 alpha-hydroxylation of 5 beta-cholestane-3 alpha,7 alpha-diol or testosterone, nor did it catalyze 7 alpha-hydroxylation of cholesterol.