The Hypoxic Stress on Erythrocytes Associated with Superoxide Formation

References

• Cerutti P. A., Fridovich I., McCord J. M. Oxy-Radicals in Molecular Biology and Pathology. Alan R. Liss, New York 1988
   Google Scholar
• Simic M. G., Taylor K. A., Ward J. F., von Sonntag C. Osygen Radicals in Biology and Medicine. Plenum Press, New York 1988
   Google Scholar
• Yoshikawa T., Furukawa Y., Wakamatsu Y., Takemura S., Tanaka H., Kondo M. Experimental hypoxia and lipid peroxidase in rats. Biochemical Medicine 1982; 27: 207–213
   PubMed Web of Science ®Google Scholar
• Hearse D. J., Humphrey S. M., Nayler W. G., Slade A., Border D. Ultra structural damage associated with deoxygenating of the anoxic myocardium. Journal of Molecular and Cellular Cardiology 1975; 7: 315–324
   PubMed Web of Science ®Google Scholar
• Stern M. D., Chien A. M., Capogrossi M. C., Pelto D. J., Lakatta E. G. Direct observation of the “oxygen paradox” in single rat ventricular myocytes. Circulation Research 1985; 56: 899–903
   PubMedGoogle Scholar
• Rifkind J. M., hang L., Heim J. M., Levy A. The role of hemoglobin in generating oxyradicals. Oxygen Radicals in Biology and Medicine, M. G. Simic, K. A. Taylor, J. F. Ward, C. von Sonntag. Plenum Press, New York 1989; 157–162
   Google Scholar
• Levy A., Zhang L., Rifkin J. M. Hemoglobin: A source of superoxide radical under hypoxic conditions. Oxy-Radicals in Molecular Biology and Pathology, P. A. Cerutti, I. Fridovich, J. M. McCord, 1988; 11–25, Alan R. Liss. New York
   Google Scholar
• Kuthan H., Ullrich V., Estabrook R. W. A quantittive test for superoxide radicals produced in biological systems. Biochemical Journal 1982; 203: 551–558
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Supcroxide dismutase: An enzymic function for erythrocuprein (hemocuprein). The Journal of Biological Chemistry 1969; 244: 6049
   PubMed Web of Science ®Google Scholar
• Azza A., Montecucco C., Richter C. The use of acetylated ferricytochrome C for the detection of superoxide radicals produced in biological membranes. Biochemical and Biophysical Research Communications 1975; 65: 597–603
   PubMedGoogle Scholar
• Tomoda A., Tsuji A., Yoneyama Y. Mechanism of hemoglobin oxidation by ferricytochrome C under aerobic and anaerobic conditions. The Journal of Biological Chemistry 1980; 255: 7978–7983
   PubMedGoogle Scholar
• Auclair C., Voisin E. Nitroblue tetrazolium reduction. Handbook of Methods for Oxygen Radical Research, R. E. Grtenwald. CRC Press, Boca Raton, Florida 1985; 123–132
   Google Scholar
• Rook G. A., Steele J., Umar S., Dockrell H. M. A simple method for the solubilisation of reduced NBT, and its use as a colorimetric assay for activation of human macrophages by gamm-interferon. Journal of immunological Methods 1985; 82: 161–167
   PubMed Web of Science ®Google Scholar
• Oberly L. W., Spits D. R. Nitroblue Tetrazolium. Handbook of Methods for Oxygen Radical Research, R. E. Greenwald. CRC Press, Boca Raton, Florida 1985; 217–220
   Google Scholar
• Gerli G. C., Beretta L., Bianchi M., Agostoni A. Erythrocyte superoxide disrnutase, catalax and glutathione peroxidase in conditions of augmented oxidant stress. Bulletin of European Physio-pathology Respiration 1981; 17: 201–205
   PubMedGoogle Scholar
• Lynch R. E., Fridovich I. Effects of superoxide on the erythrocyte membrane. The Journal of Biologicnl Chemistry 1978; 253: 1838–1845
   PubMed Web of Science ®Google Scholar
• Lynch R. E., Fridovich I. Permeation of the erythrocyte stroma by superoxide radical. The Journal of Biological Chemistry 1978; 253: 4697–4699
   PubMed Web of Science ®Google Scholar
• Rosen G. M., Barber M. J., Rauckman E. J. Disruption of erythrocyte membranal organization by superoxide. The Journal of Biological Chemistry 1983; 258: 2225–2228
   PubMed Web of Science ®Google Scholar
• Weiss S. J. The role of superoxide in the destruction of erythrocyte targets by human neutroph-ils. The Journal of biological Chemistry 1980; 255: 9912–9917
   PubMed Web of Science ®Google Scholar
• Francis J. W., Boxer L. A., Petty H. W. Optical microscopy of antibody-dependent phagocytosis and lysis of erythrocytes by living normal and chronic granulomatous disease neutrophils: A role of superoxide anions in extra-and intra-cellular lysis. Journal of Cellular Physiology 1988; 135: 1–12
   PubMedGoogle Scholar
• Cassoly R., Salhany J. M. Spectral and oxygen-release kinetic properties of human hemoglobin bound to the cytoplasmic fragment of band 3 protein in solution. Biochemical et Biophysical Acta 1983; 745: 134–139
   PubMedGoogle Scholar
• Kaul R. K., Köhler H. Interaction of hemoglobin with band 3: A review. Klinische Wochenschrift 1983; 61: 831–837
   PubMedGoogle Scholar
• Tsuneshige A., lmai K., Tyuma I. The binding of hemoglobin to red cell membrane lowers its oxygen affinity. Journal of Biochemistry 1987; 101: 695–704
   PubMedGoogle Scholar