Chiral Polychlorinated Biphenyls Are Biotransformed Enantioselectively by Mammalian Cytochrome P-450 Isozymes to Form Hydroxylated Metabolites

2009 ◽  
Vol 43 (1) ◽  
pp. 114-121 ◽  
Author(s):  
Nicholas A. Warner ◽  
Jonathan W. Martin ◽  
Charles S. Wong
Keyword(s):  
Polychlorinated Biphenyls ◽  
Hydroxylated Metabolites ◽  
Chiral Polychlorinated Biphenyls ◽  
Cytochrome P 450

Inhibition of thyroid hormone sulfation by hydroxylated metabolites of polychlorinated biphenyls

1998 ◽  
Vol 109 (1-3) ◽  
pp. 293-297 ◽  
Author(s):  
A Gerlienke Schuur ◽  
Abraham Brouwer ◽  
Åke Bergman ◽  
Michael W.H Coughtrie ◽  
Theo J Visser
Keyword(s):  
Thyroid Hormone ◽  
Polychlorinated Biphenyls ◽  
Hydroxylated Metabolites

Transformation of Chiral Polychlorinated Biphenyls (PCBs) in a Stream Food Web†

2010 ◽  
Vol 44 (8) ◽  
pp. 2836-2841 ◽  
Author(s):  
Viet D. Dang ◽  
David M. Walters ◽  
Cindy M. Lee
Keyword(s):  
Polychlorinated Biphenyls ◽  
Food Web ◽  
Chiral Polychlorinated Biphenyls

scholarly journals Ring-and N-hydroxylation of 2-acetamidofluorene by rat liver reconstituted cytochrome P-450 enzyme system

1975 ◽  
Vol 150 (3) ◽  
pp. 561-564 ◽  
Author(s):  
P D Lotlikar ◽  
K Zaleski
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Enzyme System ◽  
Partial Purification ◽  
Hydroxylated Metabolites ◽  
Triton X ◽  
Cytochrome P 450 ◽  
Ring Hydroxylation ◽  
Hydroxylation Activity ◽  
Nadph Cytochrome C Reductase

The N- and ring-hydroxylation of 2-acetamidofluorene were studied with a reconstituted cytochrome P-450 enzyme from microsomal fractions of liver from both control and 3-methylcholanthrene-pretreated rats. Proteinase treatment and Triton X-100 solubilization were two important steps for partial purification of the cytochrome P-450 fraction. Both cytochrome P-450 and NADPH-cytochrome c reductase fractions were required for optimum N- and ring-hydroxylation activity. Hydroxylation activity was determined by the source of cytochrome P-450 fraction; cytochrome P-450 fraction from pretreated animals was severalfold more active than the fraction from controls. Formation of N-hydroxylated metabolites with reconstituted systems from both control and pretreated animals was greater than that with their respective whole microsomal fractions.

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