Decrease in 2,2,6,6-tetramethyl-piperidine-1-oxyl (TEMPO) EPR signal in ozone-treated erythrocyte membranes

References

• Mehlman M.A., Borek C. Toxicity and biochemical mechanisms of ozone. Environmental Research 1987; 42: 36–53
   PubMed Web of Science ®Google Scholar
• Pryor W.A. Mechanisms of radical formation from reactions of ozone with target molecules in the lung. Free Radicals in Biology and Medicine 1994; 17: 451–465
   PubMed Web of Science ®Google Scholar
• Pryor W.A., Squadrito G.L., Friedman M. The cascade mechanism to explain ozone toxicity: the role of lipid ozonation products. Free Radicals in Biology and Medicine 1995; 19: 935–941
   PubMed Web of Science ®Google Scholar
• Church D.F., McAdams M.L., Pryor W.A. Free radical production from the ozonation of simple alkenes, fatty acid emulsions and phosphatidylcholine liposomes. Oxidative Damage and Repair: Chemical, Biological and Medical Aspects, K.J.A. Davies. Pergamon Press, Oxford 1991; 517–522, In
   Google Scholar
• Pryor W.A., Uppu R.M. A kinetic model for the competitive reactions of ozone with amino acid residues in proteins in reverse micelles. Journal of Biological Chemistry 1993; 268: 3120–3126
   PubMed Web of Science ®Google Scholar
• Berlett B.S., Levine R.L., Stadtman E.R. Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin. Journal of Biological Chemistry 1996; 271: 4177–4182
   PubMed Web of Science ®Google Scholar
• Wróbel A., Jezierski A., Gomulkiewicz J. Electron paramagnetic resonance studies of proteins in ozone-treated erythrocyte membranes. Biochemistry and Molecular Biology International 1997; 41: 349–357
   PubMedGoogle Scholar
• Dodge J.T., Mitchell C., Hanahan D.J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Archives of Biochemistry and Biophysics 1963; 100: 119–130
   PubMed Web of Science ®Google Scholar
• Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Ellman G. Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics 1959; 82: 70–77
   PubMed Web of Science ®Google Scholar
• Zahler P., Niggli V. The use of organic solvents in membrane research. Methods in Membrane Biology, E.D. Korn. Plenum Press, New York and London 1977; 1–44, In
   Google Scholar
• Gordon L.M., Curtain C.C. Electron spin resonance analysis of model and biological membranes. Methods for Studying Membrane Fluidity, R.C. Abia, C.C. Curtain, L.M. Gordon. Alan R. Liss, Inc., New York 1988; 25–88, In
   Google Scholar
• Glockner J.F., Swartz H.M., Pals M.A. Oxygen gradients in CHO cells: measurement and characterization by electron spin resonance. Journal of Cellular Physiology 1989; 140: 505–511
   PubMedGoogle Scholar
• Mitchell J.B., Samuni A., Krishna M.C., deGraff W.G., Ahn M.S., Samuni U., Russo A. Biologically active metal-independent superoxide dismutase mimics. Biochemistry 1990; 29: 2802–2807
   PubMed Web of Science ®Google Scholar
• Villarini M., Moretti M., Damiani E., Greci L., Santroni A.M., Fedeli D., Falcioni G. Detection of DNA damage in stressed trout nucleated erythrocytes using the comet assay-protection by nitroxide radicals. Free Radicals in Biology and Medicine 1998; 24: 1310–1315
   PubMed Web of Science ®Google Scholar
• Samuni A.M., Barenholz Y. Stable nitroxide radicals protect lipid acyl chains from radiation damage. Free Radicals in Biology and Medicine 1997; 22: 1165–1174
   PubMed Web of Science ®Google Scholar
• Kocherginsky N., Swartz H.M. Nitroxide Spin Labels: Reactions and Chemistry. CRC Press, Boca Raton, New York, London and Tokyo 1995
   Google Scholar
• Pryor W.A. Ozone in all its reactive splendor. Journal of Laboratory and Clinical Medicine 1993; 122: 483–486
   PubMed Web of Science ®Google Scholar
• Rosen G.M., Barber M.J., Rauckman E.J. Disruption of erythrocyte membranal organization by superoxide. Journal of Biological Chemistry 1983; 258: 2225–2228
   PubMed Web of Science ®Google Scholar
• Finkelstein E., Rosen G.M., Rauckman E.J. Superoxide-dependent reduction of nitroxides by thiols. Biochimica et Biophysica Acta 1984; 802: 90–98
   Google Scholar
• Finkelstein E., Rosen G.M., Rauckman E.J. Spin trapping of superoxide and hydroxyl radical: practical aspects. Archives of Biochemistry and Biophysics 1980; 200: 1–16
   PubMed Web of Science ®Google Scholar
• Gunther M.R., Kelman D.J., Corbett J.T., Mason R.P. Self-peroxidation of metymyoglobin results in formation of an oxygen-reactive tryptophan-centered radical. Journal of Biological Chemistry 1995; 270: 16075–16081
   PubMed Web of Science ®Google Scholar
• Barr D.P., Gunther M.R., Deterding L.J., Tomer K.B., Mason R.P. ESR Spin-trapping of a protein-derived tyrosyl radical from the reaction of cytochrome c with hydrogen peroxide. Journal of Biological Chemistry 1996; 271: 15498–15503
   PubMed Web of Science ®Google Scholar
• Gunther M.R., Tschirretguth R.A., Witkowska H.E., Fann Y.C., Barr D.P., Demontellano P.R.O., Mason R.P. Site-specific spin-trapping of tyrosine radicals in the oxidation of metmyoglobin by hydrogen peroxide. Biochemical Journal 1998; 330: 1293–1299
   PubMed Web of Science ®Google Scholar
• Miyazaki T., Yoshimura T., Mita K., Suzuki K., Watanabe M. Rate constant for reaction of vitamin C with protein radicals in gamma irradiated aqueous albumin solution at 295 K. Radiation Physics and Chemistry 1995; 45: 199–202
   Google Scholar
• Silvester J.A., Timmins G.S., Davies M.J. Photodynamically generated bovine serum albumin radicals — evidence for damage transfer and oxidation at cysteine and tryptophan residues. Free Radicals in Biology and Medicine 1998; 24: 754–766
   PubMed Web of Science ®Google Scholar
• Pietraforte D., Minetti M. Direct ESR detection of peroxynitrite-induced tyrosine-centered protein radicals in human blood plasma. biochemical Journal 1997; 325: 675–684
   PubMed Web of Science ®Google Scholar
• Dean R.T., Fu S.L., Stocker R., Davies M.J. Biochemistry and pathology of radical mediated protein oxidation. Biochemical Journal 1997; 324: 1–18
   PubMed Web of Science ®Google Scholar
• Miura Y., Utsumi H., Hamada A. Antioxidant activity of nitroxide radicals in lipid peroxidation of rat liver microsomes. Archives of Biochemistry and Biophysics 1993; 300: 148–156
   PubMed Web of Science ®Google Scholar
• Antosiewicz J., Damiani E., Jassem W., Wozniak M., Orena M., Greci L. Influence of structure on the antioxidant activity of indolinic nitroxide radicals. Free Radicals in Biology and Medicine 1997; 22: 249–255
   PubMed Web of Science ®Google Scholar