[Participation of oxygen activated species in enzymatic lipid peroxidation in biomembranes].
The participation of oxygen activated species in the induction of lipid peroxidation (LPO) in the membrane systems containing cytochrome P-450 (liver microsomes) and in the membrane fragments devoid of this hemoprotein (brain and skeletal muscle microsomes) was studied. It was shown that the rate of NADH-dependent LPO does not depend on the presence of hemoproteins and the activity of NADH-specific flavoprotein in the membranes. On the other hand, the microsomal membranes of the liver with high specific contents of b5 and P-450 cytochromes and NADPH-specific flavoprotein, had the highest rates of NADPH-dependent LPO. It was found that the most effective inhibitors of free oxygen activated species in the case of NADPH- and NADH-dependent LPO in the microsomal fractions of liver, brain and skeletal muscles are the superoxide (O ./2) anion radical inhibitors. The singlet oxygen (1O2) quenchers inhibit only NADPH-dependent LPO in the liver, however, in a far lesser degree. The hydroxyl radical (OH) scavengers had no effect on enzymatic LPO in all systems studied.
D000818:Animals; D001921:Brain / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism; D005420:Flavoproteins / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism*; D050356:Lipid Metabolism; D008297:Male; D008861:Microsomes / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D009928:Organ Specificity; D010100:Oxygen; D010545:Peroxides / Q000378:metabolism*; D051381:Rats
D003580:Cytochromes; D005420:Flavoproteins; D010545:Peroxides; D003577:Cytochrome P-450 Enzyme System; D010100:Oxygen
Ob uchastii svobodnykh aktivnykh form kisloroda v fermentnom perekisnom okislenii lipidov v biomembranakh.