Abstract
The stimulation of rat hepatic microsomal lipid peroxidation by ADP and FeCl 3 is associated with the rapid degradation of microsomal heme and the microsomal hemoprotein cytochrome P-450, with the concomitant evolution of CO. The reaction stoichiometry suggests that heme degradation occurs with the fission of one methene bridge in the tetrapyrrole ring. The process can be accelerated by increasing the cytochrome P-450 content of the incubation mixture. The product(s) of the reaction have not yet been characterized. It is suggested that this mechanism could provide an alternative pathway for hemoprotein catabolism under some normal or pathological conditions.
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