Hemoglobin-catalyzed lipid peroxidation in the presence of mercuric chloride.
In order to elucidate the possible mechanism of initiation of peroxidative processes in Hg2+-treated erythrocytes, the effect of HgCl2 on hemoglobin-catalyzed peroxidation of phospholipid liposomes was studied. It was demonstrated that HgCl2 significantly increases the rate of hemoglobin-catalyzed peroxidation. The addition of superoxide dismutase and catalase partially inhibits this effect. Furthermore, it was found that HgCl2 potentiates the hemoglobin oxidation. A suggestion was made that the acceleration of hemoglobin-catalyzed peroxidation by HgCl2 is associated at least in part with the increased production of superoxide anion radicals from hemoglobin.
D000818:Animals; D002374:Catalase / Q000494:pharmacology; D002417:Cattle; D006168:Guinea Pigs; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D008054:Lipid Peroxides / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism; D008315:Malondialdehyde / Q000378:metabolism; D008627:Mercuric Chloride; D008628:Mercury / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010743:Phospholipids / Q000378:metabolism; D013482:Superoxide Dismutase / Q000494:pharmacology
D006454:Hemoglobins; D008054:Lipid Peroxides; D008081:Liposomes; D010743:Phospholipids; D008315:Malondialdehyde; D008627:Mercuric Chloride; D002374:Catalase; D013482:Superoxide Dismutase; D008628:Mercury