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Redox Report
Communications in Free Radical Research
Volume 11, 2006 - Issue 6
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Research articles

The influence of ferrylhemoglobin and methemoglobin on the human erythrocyte membrane

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Pages 263-271 | Published online: 19 Jul 2013

REFERENCES

  • Carrell RW, Winterbourn CC, Rachmilewitz EA. Activated oxygen and haemolysis. Br J Haematol 1975; 30: 259–264.
  • Misra HP, Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem 1972; 247: 6960–6962.
  • Giulivi C, Hochstein P, Davies KJA. Hydrogen peroxide production by red blood cells. Free Radic Biol Med 1994; 16: 123–129.
  • Juliano L, Violi F, Pedersen JZ, Pratico D, Rotilio G, Balsano F. Free radical-mediated platelet activation by hemoglobin released from red blood cells. Arch Biochem Biophys 1992; 299: 220–224.
  • Kindt JT, Woods A, Martin BM, Cotter RJ, Osawa Y. Covalent alteration of the prosthetic heme of human hemoglobin by BrCC13. Cross-linking of heme to cysteine residue 93. J Biol Chem 1992; 267: 8739–8743.
  • Svistunenko DA, Patel RR Voloshchenko SV, Wilson MT. The globin-based free radical of ferryl hemoglobin is detected in normal human blood. J Biol Chem 1997; 272: 7114–7121.
  • Svistunenko DA. Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view. Biochim Biophys Ada 2005; 1707: 127–155.
  • Giulivi C, Cadenas E, Heme protein radicals: formation, fate and biological consequences. Free Radic Biol Med 1998; 24: 269–279.
  • McArthur KM, Davies MJ. Detection and reactions of the globin radical in haemoglobin. Biochim Biophys Acta 1993; 1202: 173–181.
  • Winterbourn CC. Oxidative reactions of hemoglobin. Methods Enzymol 1990; 186: 265–272.
  • Deterding LJ, Ramirez DC, Dubin RP, Mason KB, Tomer KB. Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical. J Biol Chem 2004; 279: 11600–11607.
  • Patel RP, Svistunenko DA, Darley-Usmar VM, Symons MCR, Wilson MT. Redox cycling of human methaemoglobin by H202 yields persistent ferryl iron and protein based radicals. Free Radic Res 1996; 25: 117–123.
  • Gebicki JM. Protein hydroperoxides as new reactive oxygen species, Redox Report 1997; 3: 99-110.
  • Johnson RM, Goyette Jr G, Ravindranath Y, Ho YS. Hemoglobin autoxidation and regulation of endogenous H202 levels in erythrocytes. Free Radic Biol Med 2005; 39: 1407–1417.
  • Abassi ZA, Hoffman A, Better OS. Acute renal failure complicating muscle crush injury. Semin Nephrol 1998; 18: 558–565.
  • Galaris D, Eddy L, Arduini A, Cadenas E, Hochstein P. Mechanisms of reoxygenation injury in myocardial infarction: implications of a myoglobin redox cycle. Biochem Biophys Res Commun 1989; 160: 1162–1168.
  • Arduini A, Eddy L, Hochstein P. Detection of ferrylmyoglobin in the isolated ischemic rat heart. Free Radic Biol Med 1990; 9: 511–513.
  • Miura T, Muraoka S, Ogiso T. Relationship between protein damage and ferrylmyoglobin. Biochem Mount 1995; 36: 587–594.
  • Miura T, Muraoka S, Ogiso T. Inactivation of glyceraldehyde-3 - phosphate dehydrogenase by ferrylmyoglobin. Chemicobiol Int 1997; 107: 173–183.
  • Ostald H, Andersen HJ, Davies MJ. Formation of long-lived radicals on proteins by radical transfer from heme enzymes - a common process? Arch Biochem Biophys 1999; 362: 105–112.
  • Irvin JA, Ostald H, Davies MJ. Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Arch Biochem Biophys 1999; 362: 94–104.
  • Dodge J, Mitchell C, Hanahan D. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 1963; 100: 119–130.
  • Lowry OH, Rosenbrough NJ, Farr L, Randal RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265–275.
  • Drabkin L. The crystallographic and optical properties of the hemoglobin of man. J Biol Chem 1946; 164: 703–723.
  • Szweda-Lewandowska Z. Role of water and ethanol radicals in the radiation destruction of human deoxyhemoglobin. Radiat Environ Biophys 1986; 25: 201–212.
  • Ellman GL, Courtney KD, Andres Jr V, Feather-Stone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 1961; 7: 88–95.
  • Stocks J, Dromandy TL, The autoxidation of human red cell lipids induced by hydrogen peroxide. Br J Haematol 1971; 20: 95–111.
  • Svistunenko DA. An EPR study of the peroxyl radicals induced by hydrogen peroxide in the haem proteins. Biochim Biophys Ada 2001; 1546: 365–378.
  • Frenkel EJ, Roelofsen B, Brodbeck U, van Deenen LL, Ott P. Lipid-protein interactions in human erythrocyte-membrane acetylcholinesterase. Modulation of enzyme activity by lipids. Eur J Biochem 1980; 109: 377–382.
  • Soszynski M, Bartosz G. Decrease in accessible thiols as an index of oxidative damage to membrane proteins. Free Radic Biol Med 1997; 23: 463–469.
  • Kanner J, Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Arch Biochem Biophys 1985; 237: 314–321.
  • D'Agnillo F, Alayash Al. Interactions of hemoglobin with hydrogen peroxide alters thiol levels and course of endothelial cell death. Am J Physiol 2000; 279: H1880–H1889.
  • Sztiller M, Puchala M. The influence of metmyoglobin and ferrylmyoglobin on the human erythrocyte membrane. Cell Mol Biol Lett 2003; 8: 337–342.

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