Enzymatic detoxication of DDT to DDD by rat liver: Effects of some inducers and inhibitors of cytochrome P-450 enzyme system

1987 ◽  
Vol 38 (3) ◽  
pp. 449-455 ◽  
Author(s):  
S. S. A. Zaidi ◽  
B. D. Banerjee
Keyword(s):  
Rat Liver ◽  
Enzyme System ◽  
Cytochrome P 450

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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