Abstract
A new method was employed for the purification of cytochrome P-450 from rat liver microsomes. The purified cytochrome was essentially free from possible contaminants and the recovery and degree of purification were high. Although 15% of the original P-450 was recovered through the purification procedure used, only 0.8% of the total original microsomal ethanol oxidation activity was associated with this fraction. Addition of this purified fraction to other fractions isolated did not further stimulate ethanol oxidation. The component of rat liver microsomes that was found most efficient in the oxidation of ethanol was the mixture of catalase and NADPH - cytochrome c - reductase. It is concluded that highly purified cytochrome P-450 by itself does not oxidize ethanol to any appreciable degree.
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