References
- White C. T., Murray A. J., Greene J. R., Smith D. J., Medina F., Makovec G. T., Martin E. J., Bolin R. B. Toxicity of human hemoglobin solution infused into rabbits. J Labor Clin Med 1986; 108: 121–131
- Sadrzadeh S. M.H., Eaton J. W. Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate. J Clin Invest 1988; 82: 1510–1515
- Wallace W. J., Houtchens R. A., Maxwell J. C., Caughey W. S. Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J Biol Chem 1982; 257: 4966–4977
- Watkins J A., Kawanishi S., WCaughey S. Autoxidation reactions of hemoglobin a free from other red cell components: a minimal mechanism. Biochem Biophys Res Comm 1985; 132: 742–748
- Sadrzadeh S. M.H., Graf E., Ranter S. S., Hallaway P. E., Eaton J. W. Hemoglobin: a biological Fenton reagent. J Biol Chem 1984; 259: 14354–14356
- Puppo A., Halliwell B. Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Biochem J 1988; 249: 185–190
- Gutteridge J. M.C. Iron promoters of the fenton reaction and lipid peroxidation can be released from hemoglobin by peroxidase. FEBS Letters 1986; 201: 291–295
- Samaja M., Rovida E., Niggeler M., Perrella M., Bernardi Rossi L. The dissociation of carbon monoxide from hemoglobin intermediates. J Biol Chem 1987; 262: 4528–4533
- Van Assendelft O. W. Spectrophotometry of haemoglobin derivatives. Royal Vangorcum Ltd., Asse, NL 1970
- Christensen S. M., Medina F., Winslow R. M., Snell S. M., Zegna A., Marini M. A. Preparation of human hemoglobin A0 for possible use as a substitute. J Biochem Biophys Meth 1988; 17: 143–154
- Snyder S. R., Welty E. V., Walder R. Y., Williams L. A., Walder J. A. HbxL99α: a hemoglobin derivative that is cross-linked between the a subunits is useful as a blood substitute. Proc Natl Acad Sci USA 1987; 84: 7280–7284
- Roughton F. J.W., Severinghaus J. W. Accurate determination of O 2 dissociation curve of human above 98.7% saturation with data on O2 solubility in unmodified human blood from 0° to 37°C. J Appl Physiol 1973; 35: 861–869
- McCord J. M., Fridovich I. The reduction of cytochrome c by milk xanthine oxidase. J Biol Chem 1968; 243: 5753–5760
- Rachmilewitz E. A., Peisach J., Blumberg W. E. Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives. J Biol Chem 1971; 246: 3356–3366
- Yusa K., Shikama K. Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: involvement of ferryl intermediate. Biochemistry 1987; 26: 6684–6688
- Whitburn K. D. The interaction of oxymyoglobin with hydrogen peroxide: the formation of ferrylmyoglobin at moderate excesses of hydrogen peroxide. Arch Biochem Biophys 1987; 253: 419–430
- Prasad M. R., Engelman R. M., Jones R. M., Das D. K. Effects of oxyradicals on oxymyoglobin. Deoxygenation, haem removal and iron release. Biochem J 1989; 263: 731–736
- Barksdale A. D., Rosenberg A. Thermodynamic characterization of subunit association in liganded ferrohemoglobin. J Biol Chem 1978; 253: 4881–4885
- Samaja M., Rovida E. The dissociation of carbon monoxide from the alpha and the subunits of human carbonmonoxy hemoglobin. Biochem Biophys Res Comm 1987; 148: 1196–1201
- Yang T., Olsen K. W. The effect of crosslinking by bis (3–5-dibromosalicyl) on the autoxidation of hemoglobin. Biochem Biophys Res Comm 1989; 163: 733–738