Lipid peroxidation of rat liver microsomes.
1. The NADPH-dependent lipid peroxidation process was studied with microsomes and also the effects of addition of superoxide dismutase, catalase and thiourea. Only catalase and thiourea were able to inhibit lipid peroxidation. It seems that the initiating radical is the OH. radical formed by the Fenton reaction. 2. During lipid peroxidation glucose-6-phosphatase is inactivated, whilst the microsomal enzyme palmitoyl-CoA hydrolase is practically not affected. Because glucose-6-phosphatase activity decreases during ageing and palmitoyl-CoA hydrolase does not, a possible relationship with the ageing process is thought to exist. 3. Chromolipids are formed by the NADPH-dependent lipid peroxidation. These chromolipids have the same excitation-emission spectra as described for lipofuscin. The formation of these chromolipids is blocked by the addition of catalase and thiourea. 4. High-molecular weight proteins are formed during the NADPH-dependent lipid peroxidation. This process can be associated with the inactivation of enzymes. Also polymerisation is prevented by catalase and thiourea.
D000818:Animals; D002374:Catalase / Q000494:pharmacology; D008054:Lipid Peroxides / Q000096:biosynthesis*; D008315:Malondialdehyde / Q000032:analysis; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D010170:Palmitoyl-CoA Hydrolase / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D014176:Protein Biosynthesis; D051381:Rats; D013050:Spectrometry, Fluorescence; D013890:Thiourea / Q000494:pharmacology
D008054:Lipid Peroxides; D008315:Malondialdehyde; D009249:NADP; D002374:Catalase; D010170:Palmitoyl-CoA Hydrolase; D010744:Phosphoric Monoester Hydrolases; D013890:Thiourea