Absence of Hemoprotein-Associated Free Radical Events Following Oxidant Challenge of Crosslinked Hemoglobin–Superoxide Dismutase Catalase

• Published in: Free radical biology & medicine Vol. 24; no. 6; pp. 906 - 912
• Main Authors: D’Agnillo, Felice, Chang, Thomas M.S
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 1998
• Subjects: Animals; BHT; Blood Substitutes; butylated hydroxytoluene; CAT; Catalase; Catalase - chemical synthesis; Catalase - chemistry; Catalase - drug effects; Cattle; Cross-Linking Reagents - chemistry; DHBA; dihydroxybenzoate; Ferrozine - metabolism; Ferrylhemoglobin; Free radical; Free Radical Scavengers - antagonists & inhibitors; Free Radical Scavengers - metabolism; Glutaral - chemistry; Glutaraldehyde; H 2O 2; Hemoglobin; Hemoglobins - chemical synthesis; Hemoglobins - chemistry; Hemoglobins - drug effects; Hemoglobins - metabolism; Hydrogen peroxide; Hydrogen Peroxide - pharmacology; Hydroxyl radical; Hydroxylation; Iron - analysis; Iron - metabolism; Lipid peroxidation; Lipid Peroxidation - drug effects; Liposomes - chemistry; Models, Biological; O 2; OH; Oxidation-Reduction - drug effects; Phospholipids - chemistry; PolyHb; PolyHb-SOD-CAT; Polymerization; polymerized hemoglobin; polymerized hemoglobin, SOD, and catalase; polyunsaturated fatty acid; PUFA; Salicylic Acid - analysis; Salicylic Acid - metabolism; SOD; Superoxide; superoxide anion radical or superoxide; Superoxide dismutase; Superoxide Dismutase - chemical synthesis; Superoxide Dismutase - chemistry; Superoxide Dismutase - drug effects; Superoxides - chemical synthesis; Superoxides - pharmacology; TBA; TCA; thiobarbituric acid; trichloroacetic acid; Xanthine Oxidase - chemistry; O 2; Hydrogen peroxide; PUFA; Lipid peroxidation; Polymerization; Superoxide dismutase; SOD; Superoxide; PolyHb-SOD-CAT; Free radical; BHT; H 2O 2; TBA; Glutaraldehyde; TCA; Catalase; PolyHb; CAT; Hemoglobin; OH; Hb; Ferrylhemoglobin; DHBA; Hydroxyl radical
• ISSN: 0891-5849
• DOI: 10.1016/S0891-5849(97)00374-2

Crosslinking hemoglobin with superoxide dismutase and catalase (PolyHb-SOD-CAT) helps to limit free radical reactivity of modified hemoglobin red blood cell substitutes. In the present study, in vitro oxidant challenge experiments were performed with exogenous hydrogen peroxide (H 2O 2) and xanthine oxidase-derived superoxide (O 2 ·−). PolyHb-SOD-CAT was compared to PolyHb for the presence of secondary hemoprotein-free radical events. PolyHb-SOD-CAT prevents ferrylhemoglobin formation, measured as Na 2S-induced absorbance at 620 nm. Similarly, PolyHb-SOD-CAT inhibited ferrozine-detectable iron release at high oxidant-heme ratios. The formation of oxygen radicals, monitored by salicylate hydroxylation, was prevented at high oxidant–heme ratios with PolyHb-SOD-CAT. The peroxidation of liposomal membranes was also inhibited in PolyHb-SOD-CAT mixtures subject to oxidant challenge. These results show that PolyHb-SOD-CAT prevents secondary hemoprotein-associated free radical events. This new type of modified hemoglobin oxygen carrier with antioxidant activity may reduce the potential toxicity of hemoglobin-based substitutes in certain applications, especially during reperfusion of ischemic tissues.