Abstract
Cytochrome P-450 in whole liver homogenates, which contain an appreciable amount of hemoglobin, is detected by dithionite-difference spectroscopy of CO-bubbled homogenates. The molar extinction difference of cytocrhome P-450 by this method was determined to be 104 m m −1cm −1 by comparative observations of the absorbance change in the dithionite- and CO-difference spectra of the membrane-bound hemoprotein. The content of cytochrome P-450 in normal rat liver was estimated to be 50 nmol/g wet weight of liver, and increased significantly after pretreatment of the animals with either phenobarbital or 3-methylcholanthrene.
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