Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important.
|Number of pages||4|
|Journal||Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism|
|Publication status||Published - Jul 9 1985|
- (Brain and liver microsome)
- Heme-nonapeptide inhibitor
- Lipid peroxidation
ASJC Scopus subject areas