Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c.
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 blocker 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.
Vodnyánszky
L
L
Marton
A
A
Venekei
I
I
Végh
M
M
Blázovits
A
A
Kittel
A
A
Horváth
I
I
D000818:Animals; D001921:Brain / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism* / Q000494:pharmacology; D045304:Cytochromes c; D006418:Heme / Q000378:metabolism* / Q000494:pharmacology; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010101:Oxygen Consumption; D010446:Peptide Fragments / Q000378:metabolism* / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D003574:Cytochrome c Group; D008054:Lipid Peroxides; D010446:Peptide Fragments; C046027:heme nonapeptide; D009243:NAD; D006418:Heme; D009249:NADP; D045304:Cytochromes c