Abstract
We describe the resolution and partial purification of two minor forms of cytochrome P-450 from liver microsomes of rabbits treated with 2,3,7,8-tetrachlorodibenzo- p -dioxin. Both forms have different electrophoretic mobilities when compared to the major form of cytochrome P-450 isolated from this source. The two cytochromes show different activities with several substrates. One form is very active in the hydroxylation of benzo( a )pyrene when reconstituted with highly purified NADPH-cytochrome P-450 reductase.
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More From: Biochemical and Biophysical Research Communications
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