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Journal of Lipid Research, Vol 27, 807-812, Copyright © 1986 by Lipid Research, Inc.

ARTICLES

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

H Bostrom

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.
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				K. Lundell, R. Hansson, and K. Wikvall Cloning and Expression of a Pig Liver Taurochenodeoxycholic Acid 6alpha -Hydroxylase (CYP4A21). A NOVEL MEMBER OF THE CYP4A SUBFAMILY J. Biol. Chem., March 23, 2001; 276(13): 9606 - 9612. [Abstract] [Full Text] [PDF]