Abstract
Isolated rat liver microsomes were subjected to enzymatic or non-enzymatic lipid peroxidation in vitro . NADPH-dependent cytochrome c reductase activity was released from the microsomes into the media during peroxidation. This activity could be recovered from the media by DEAE-cellulose chromatography. The recovered enzyme retained high activity for the reduction of cytochrome c and a lower level of activity for the reduction of cytochrome P-450. The active fractions were capable of enzymatically supporting the peroxidation of isolated mitochondria in the presence of organically complexed Fe +3 and NADPH, and in this respect the specific activity was found to be about ten times higher than in microsomes.
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