메뉴 건너뛰기




Volumn 272, Issue 2 16-2, 1997, Pages

Air blast-induced pulmonary oxidative stress: Interplay among hemoglobin, antioxidants, and lipid peroxidation

Author keywords

antioxidant depletion; blast overpressure; hemoglobin oxidation; lung injury; prooxidants

Indexed keywords

ANTIOXIDANT; HEMOGLOBIN;

EID: 0030938695     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1997.272.2.l320     Document Type: Article
Times cited : (55)

References (67)
  • 2
    • 0028154760 scopus 로고
    • Vitamin C, dehydroascorbate, and uric acid in tissues and serum: High-performance liquid chromatography
    • Barja, G., and A. Hernanz. Vitamin C, dehydroascorbate, and uric acid in tissues and serum: high-performance liquid chromatography. Methods Enzymol. 234: 331-337, 1994.
    • (1994) Methods Enzymol. , vol.234 , pp. 331-337
    • Barja, G.1    Hernanz, A.2
  • 3
    • 0020317282 scopus 로고
    • Reactions of adriamycin with haemoglobin. Superoxide dismutase inderectly inhibits reactions of the adriamycin semiquinone
    • Bates, D. A., and C. C. Winterbourn. Reactions of adriamycin with haemoglobin. Superoxide dismutase inderectly inhibits reactions of the adriamycin semiquinone. Biochem. J. 203: 155-160, 1982.
    • (1982) Biochem. J. , vol.203 , pp. 155-160
    • Bates, D.A.1    Winterbourn, C.C.2
  • 4
    • 0028171330 scopus 로고
    • Redox processes in malaria and other parasitic diseases. Determination of inspectrumllular glutathione
    • Becker, K., M. Gui, A. Traxler, C. Kirsten, and R. H. Schirmer. Redox processes in malaria and other parasitic diseases. Determination of inspectrumllular glutathione. Biochemistry 102: 389-395, 1994.
    • (1994) Biochemistry , vol.102 , pp. 389-395
    • Becker, K.1    Gui, M.2    Traxler, A.3    Kirsten, C.4    Schirmer, R.H.5
  • 5
    • 0000485960 scopus 로고
    • Physiological effects of blast in air and water
    • Washington, DC: US Government Printing Office
    • Benziner, T. Physiological effects of blast in air and water. In: German Aviation Medicine, World War II. Washington, DC: US Government Printing Office, 1950, p. 1225-1259.
    • (1950) German Aviation Medicine, World War II , pp. 1225-1259
    • Benziner, T.1
  • 6
    • 0021914279 scopus 로고
    • Oxygen-free radicals and lipid peroxidation in adult respiratory distress syndrome
    • Bertrand, Y. Oxygen-free radicals and lipid peroxidation in adult respiratory distress syndrome. Intensive Care Med. 11: 56-60, 1985.
    • (1985) Intensive Care Med. , vol.11 , pp. 56-60
    • Bertrand, Y.1
  • 7
    • 0021253104 scopus 로고
    • Interaction of granulocytes with the lungs
    • Brigham, K. L., and B. Meyrick. Interaction of granulocytes with the lungs. Circ. Res. 54: 623-635, 1984.
    • (1984) Circ. Res. , vol.54 , pp. 623-635
    • Brigham, K.L.1    Meyrick, B.2
  • 8
    • 0027456398 scopus 로고
    • The ultrastructure of rat lung following acute primary blast injury
    • Brown, R. F. R., G. J. Cooper, and R. L. Maynard. The ultrastructure of rat lung following acute primary blast injury. Int. J. Exp. Pathol. 74: 151-162, 1993.
    • (1993) Int. J. Exp. Pathol. , vol.74 , pp. 151-162
    • Brown, R.F.R.1    Cooper, G.J.2    Maynard, R.L.3
  • 9
    • 0025673729 scopus 로고
    • Ascorbate oxidation: UV absorbance of ascorbate and ESR spectroscopy of the ascorbyl radical as assays for iron
    • Buettner, G. R. Ascorbate oxidation: UV absorbance of ascorbate and ESR spectroscopy of the ascorbyl radical as assays for iron. Free Radical Res. Commun. 10: 5-9, 1990.
    • (1990) Free Radical Res. Commun. , vol.10 , pp. 5-9
    • Buettner, G.R.1
  • 10
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, α-tocopherol, and ascorbate
    • Buettner, G. R. The pecking order of free radicals and antioxidants: lipid peroxidation, α-tocopherol, and ascorbate. Arch. Biochem. Biophys. 300: 535-543, 1993.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 12
    • 0028117970 scopus 로고
    • Redox conversions of methemoglobin during redox cycling of quinones and aromatic nitrocompaunds
    • Cenas, N., and K. Ollinger. Redox conversions of methemoglobin during redox cycling of quinones and aromatic nitrocompaunds. Arch. Biochem. Biophys. 315: 170-176, 1994.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 170-176
    • Cenas, N.1    Ollinger, K.2
  • 14
    • 3042934967 scopus 로고
    • Tissues sulfhydril groups
    • Ellman, G. L. Tissues sulfhydril groups. Arch. Biochem. Biophys. 82: 70-77, 1952.
    • (1952) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 15
    • 0029961007 scopus 로고    scopus 로고
    • Antioxidant depletion, lipid peroxidation, and impairment of calcium transport induced by air-blast overpressure in rat lungs
    • Elsayed, N. M., Y. Y. Tyurina, V. A. Tyurin, E. V. Menshikova, E. R. Kisin, and V. E. Kagan. Antioxidant depletion, lipid peroxidation, and impairment of calcium transport induced by air-blast overpressure in rat lungs. Exp. Lung Res. 22: 179-200, 1996.
    • (1996) Exp. Lung Res. , vol.22 , pp. 179-200
    • Elsayed, N.M.1    Tyurina, Y.Y.2    Tyurin, V.A.3    Menshikova, E.V.4    Kisin, E.R.5    Kagan, V.E.6
  • 16
    • 0016705164 scopus 로고
    • Kinetics of ferrihemoglobin formation by some reducing agents, and the role of hydrogen peroxide
    • Eyer, P., H. Hertle, M. Kiase, and G. Klein. Kinetics of ferrihemoglobin formation by some reducing agents, and the role of hydrogen peroxide. Mol. Pharmacol. 11: 326-334, 1975.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 326-334
    • Eyer, P.1    Hertle, H.2    Kiase, M.3    Klein, G.4
  • 17
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissue
    • Folch, J., M. Lees, and G. H. Sloan-Starley. A simple method for the isolation and purification of total lipids from animal tissue. J. Biol. Chem. 226: 497-509, 1957.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloan-Starley, G.H.3
  • 18
    • 0024444665 scopus 로고
    • Redox cycling of myoglobin and ascorbate: A potential protective mechanism against oxidative reperfusion injury in muscle
    • Galaris, D., E. Cadenas, and P. Hochstein. Redox cycling of myoglobin and ascorbate: a potential protective mechanism against oxidative reperfusion injury in muscle. Arch. Biochem. Biophys. 273: 497-504, 1989.
    • (1989) Arch. Biochem. Biophys. , vol.273 , pp. 497-504
    • Galaris, D.1    Cadenas, E.2    Hochstein, P.3
  • 19
    • 0027482489 scopus 로고
    • The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects
    • Giulivi, C., and E. Cadenas. The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects. FEBS Lett. 332: 287-290, 1993.
    • (1993) FEBS Lett. , vol.332 , pp. 287-290
    • Giulivi, C.1    Cadenas, E.2
  • 21
    • 0029069277 scopus 로고
    • Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: A protective mechanism against ferryl hemoprotein-induced oxidation
    • Gorbunov, N. V., A. N. Osipov, B. W. Day, B. Zayas-Rivera, V. E. Kagan, and N. M. Elsayed. Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: a protective mechanism against ferryl hemoprotein-induced oxidation. Biochemistry 34: 6689-6699, 1995.
    • (1995) Biochemistry , vol.34 , pp. 6689-6699
    • Gorbunov, N.V.1    Osipov, A.N.2    Day, B.W.3    Zayas-Rivera, B.4    Kagan, V.E.5    Elsayed, N.M.6
  • 23
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease
    • Halliwell, B., and J. M. C. Gutteridge. Role of free radicals and catalytic metal ions in human disease. Methods Enzymol. 186: 1-85, 1990.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 25
    • 0023693165 scopus 로고
    • The generation of ferryl or hydroxyl radicals during interactions of haemoproteins with hydrogen peroxide
    • Harel, S., and J. Kanner. The generation of ferryl or hydroxyl radicals during interactions of haemoproteins with hydrogen peroxide. Free Radical Res. Commun. 5: 21-33, 1988.
    • (1988) Free Radical Res. Commun. , vol.5 , pp. 21-33
    • Harel, S.1    Kanner, J.2
  • 26
    • 0014010536 scopus 로고
    • Electron spin resonance studies of the denaturation of oxy- and methemoglobin. Spectra and solution interaction
    • Hollocher, T. C. Electron spin resonance studies of the denaturation of oxy- and methemoglobin. Spectra and solution interaction. J. Biol. Chem. 241: 1958-1968, 1966.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1958-1968
    • Hollocher, T.C.1
  • 27
    • 0015237988 scopus 로고
    • Catalysis of methaemoglobin reduction by erythrocyte cytochrome b5 and cytochrome b5 reductase
    • Hultquist, D. E., and P. G. Passon. Catalysis of methaemoglobin reduction by erythrocyte cytochrome b5 and cytochrome b5 reductase (Abstract). Nature Lond. 229: 252, 1971.
    • (1971) Nature Lond. , vol.229 , pp. 252
    • Hultquist, D.E.1    Passon, P.G.2
  • 28
    • 0027089843 scopus 로고
    • Free radical-mediated platelet activation by hemoglobin released from red blood cells
    • Iuliano, L., J. Z. Pedersen, D. Pratico, G. Rotilio, and F. Balsano. Free radical-mediated platelet activation by hemoglobin released from red blood cells. Arch. Biochem. Biophys. 299: 220-224, 1992.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 220-224
    • Iuliano, L.1    Pedersen, J.Z.2    Pratico, D.3    Rotilio, G.4    Balsano, F.5
  • 29
    • 0028986455 scopus 로고
    • Alpha-tocopherol mediated peroxidation in the copper (II) and metmyoglobin induced oxidation of human low density lipoprotein: The influence of lipid hydroperoxides
    • Iwatsuki, M., E. Niki, D. Stone, and U. M. Darley-Usmar. Alpha-tocopherol mediated peroxidation in the copper (II) and metmyoglobin induced oxidation of human low density lipoprotein: the influence of lipid hydroperoxides. FEBS Lett. 360: 271-276, 1995.
    • (1995) FEBS Lett. , vol.360 , pp. 271-276
    • Iwatsuki, M.1    Niki, E.2    Stone, D.3    Darley-Usmar, U.M.4
  • 30
    • 0023916897 scopus 로고
    • Re-expansion pulmonary edema: A potential role for free radicals in its pathogenesis
    • Jackson, R. M., C. F. Veal, B. Alexander, and J. D. Fulmer. Re-expansion pulmonary edema: a potential role for free radicals in its pathogenesis. Am. Rev. Respir. Dis. 137: 1165-1171, 1988.
    • (1988) Am. Rev. Respir. Dis. , vol.137 , pp. 1165-1171
    • Jackson, R.M.1    Veal, C.F.2    Alexander, B.3    Fulmer, J.D.4
  • 32
    • 0028284759 scopus 로고
    • Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates
    • Kelman, D. J., J. A. DeGray, and R. P. Mason. Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. J. Biol. Chem. 269: 7458-7463, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7458-7463
    • Kelman, D.J.1    Degray, J.A.2    Mason, R.P.3
  • 33
    • 0000952295 scopus 로고
    • The mechanism of metmyoglobin oxidation
    • Kelso King, N., and M. E. Winfield. The mechanism of metmyoglobin oxidation. J. Biol. Chem. 238: 1520-1528, 1963.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1520-1528
    • Kelso King, N.1    Winfield, M.E.2
  • 34
    • 0019418785 scopus 로고
    • Properties of methemoglobin reductase and kinetic study of methemoglobin reduction
    • Kuma, F. Properties of methemoglobin reductase and kinetic study of methemoglobin reduction. J. Biol. Chem. 256: 5518-5523, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5518-5523
    • Kuma, F.1
  • 36
    • 0023630139 scopus 로고
    • Role of hydroxyl radicals derived from granulocytes in lung injury induced by phorbol myristate acetate
    • Kuroda, M., K. Murakami, and Y. Ishikawa. Role of hydroxyl radicals derived from granulocytes in lung injury induced by phorbol myristate acetate. Am. Rev. Respir. Dis. 136: 1435-1444, 1987.
    • (1987) Am. Rev. Respir. Dis. , vol.136 , pp. 1435-1444
    • Kuroda, M.1    Murakami, K.2    Ishikawa, Y.3
  • 37
    • 0022552575 scopus 로고
    • Simultaneous determination of tocopherols, ubiquinols, and ubiquinones in blood, plasma, tissue homogenates, and subcellular fractions
    • Lang, J. K., K. Gohil, and L. Packer. Simultaneous determination of tocopherols, ubiquinols, and ubiquinones in blood, plasma, tissue homogenates, and subcellular fractions. Anal. Biochem. 157: 106-116, 1986.
    • (1986) Anal. Biochem. , vol.157 , pp. 106-116
    • Lang, J.K.1    Gohil, K.2    Packer, L.3
  • 39
    • 0028220123 scopus 로고
    • Oxidation of spin trap 5,5-dimethyl-1-pyrolline-1-oxide in an electron paramagnetic resonanse study of the reaction of methemoglobin with hydrogen peroxide
    • Mao, G. D., P. D. Thomas, and M. J. Poznansky. Oxidation of spin trap 5,5-dimethyl-1-pyrolline-1-oxide in an electron paramagnetic resonanse study of the reaction of methemoglobin with hydrogen peroxide. Free Radical Biol. Med. 16: 493-500, 1994.
    • (1994) Free Radical Biol. Med. , vol.16 , pp. 493-500
    • Mao, G.D.1    Thomas, P.D.2    Poznansky, M.J.3
  • 40
    • 0025040580 scopus 로고
    • Thiyl free radical metabolites of thiol drugs, glutathione, and proteins
    • Mason, R. P., and D. N. Rao. Thiyl free radical metabolites of thiol drugs, glutathione, and proteins. Methods Enzymol. 186: 318-329, 1990.
    • (1990) Methods Enzymol. , vol.186 , pp. 318-329
    • Mason, R.P.1    Rao, D.N.2
  • 41
    • 0028805076 scopus 로고
    • Ascorbic acid recycling enhances the antioxidant reserve of human erythrocytes
    • May, J. M., Z. Qu, and R. R. Whitesell. Ascorbic acid recycling enhances the antioxidant reserve of human erythrocytes. Biochemistry 34: 12721-12728, 1995.
    • (1995) Biochemistry , vol.34 , pp. 12721-12728
    • May, J.M.1    Qu, Z.2    Whitesell, R.R.3
  • 42
    • 0028900182 scopus 로고
    • Heme protein-mediated renal injury: A protective role for 21-aminosteroids in vitro and in vivo
    • Nath, K. A., J. Balla, A. J. Croatt, and G. M. Vercellotti. Heme protein-mediated renal injury: a protective role for 21-aminosteroids in vitro and in vivo. Kidney Int. 47: 592-602, 1995.
    • (1995) Kidney Int. , vol.47 , pp. 592-602
    • Nath, K.A.1    Balla, J.2    Croatt, A.J.3    Vercellotti, G.M.4
  • 43
    • 0025082043 scopus 로고
    • Free radical initiators as source of water- or lipid-soluble peroxyl radicals
    • Niki, E. Free radical initiators as source of water- or lipid-soluble peroxyl radicals. Methods Enzymol. 186: 100-108, 1990.
    • (1990) Methods Enzymol. , vol.186 , pp. 100-108
    • Niki, E.1
  • 44
    • 0027321369 scopus 로고
    • Chemiluminescence from activated heme compounds detected in the reaction of various xenobiotics with oxyhemoglobin: Comparison with several heme/hydrogen peroxide system
    • Nohl, H., and K. Stolze. Chemiluminescence from activated heme compounds detected in the reaction of various xenobiotics with oxyhemoglobin: comparison with several heme/hydrogen peroxide system. Free Radical Biol. Med. 15: 257-263, 1993.
    • (1993) Free Radical Biol. Med. , vol.15 , pp. 257-263
    • Nohl, H.1    Stolze, K.2
  • 45
    • 0025294118 scopus 로고
    • Inhibition by free-radical scavenger of ascorbate-induced hemoglobin denaturation in glucose-6-phosphate dehydrogenase deficient erythrocytes
    • Papandreou, P. T., and E. T. Rakitzis. Inhibition by free-radical scavenger of ascorbate-induced hemoglobin denaturation in glucose-6-phosphate dehydrogenase deficient erythrocytes. Clin. Chim. Acta 189: 253-254, 1990.
    • (1990) Clin. Chim. Acta , vol.189 , pp. 253-254
    • Papandreou, P.T.1    Rakitzis, E.T.2
  • 46
    • 0038360739 scopus 로고
    • Primary blast injury and basic research: A brief history
    • edited by R. Bellamy and R. Zaitchuk. Washington, DC: Office of the Surgeon General, Department of the Army, USA
    • Phillips III, Y. Y., and D. R. Richmond. Primary blast injury and basic research: a brief history. In: Textbook of Military Medicine (Conventional Warfare, Ballistic, Blast, and Burn Injuries), edited by R. Bellamy and R. Zaitchuk. Washington, DC: Office of the Surgeon General, Department of the Army, USA, 1991, vol. 5, p. 221-240.
    • (1991) Textbook of Military Medicine (Conventional Warfare, Ballistic, Blast, and Burn Injuries) , vol.5 , pp. 221-240
    • Phillips III, Y.Y.1    Richmond, D.R.2
  • 47
    • 0025352479 scopus 로고
    • Ascorbate- and hemoglobin-dependent brain chemiluminescence
    • Prat, A. G., and J. F. Turrents. Ascorbate- and hemoglobin-dependent brain chemiluminescence. Free Radical Biol. Med. 8: 319-325, 1990.
    • (1990) Free Radical Biol. Med. , vol.8 , pp. 319-325
    • Prat, A.G.1    Turrents, J.F.2
  • 48
    • 0021288839 scopus 로고
    • Spectrophotometric detection of lipid conjugated dienes
    • Recknagel, R. O., and E. A. Glende, Jr. Spectrophotometric detection of lipid conjugated dienes. Methods Enzymol. 105: 331-337, 1984.
    • (1984) Methods Enzymol. , vol.105 , pp. 331-337
    • Recknagel, R.O.1    Glende Jr., E.A.2
  • 49
    • 0027298460 scopus 로고
    • Neurotoxicity of hemoglobin in cortical cell culture
    • Regan, R. F., and S. S. Panter. Neurotoxicity of hemoglobin in cortical cell culture. Neurosci. Lett. 153: 219-222, 1993.
    • (1993) Neurosci. Lett. , vol.153 , pp. 219-222
    • Regan, R.F.1    Panter, S.S.2
  • 50
    • 0026509008 scopus 로고
    • The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formations of thiyl radical intermediates
    • Romero, F. J., I. Ordonez, A. Arduini, and E. Cadenas. The reactivity of thiols and disulfides with different redox states of myoglobin. Redox and addition reactions and formations of thiyl radical intermediates. J. Biol. Chem. 267: 1680-1688, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1680-1688
    • Romero, F.J.1    Ordonez, I.2    Arduini, A.3    Cadenas, E.4
  • 52
    • 0024242512 scopus 로고
    • Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate
    • Sadrzadeh, S. M., and J. W. Eaton. Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate. J. Clin. Invest. 82: 1510-1515, 1988.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1510-1515
    • Sadrzadeh, S.M.1    Eaton, J.W.2
  • 56
    • 0025761002 scopus 로고
    • Hemoglobin potentiates oxidant injury in isolated rat lungs
    • Heart Circ. Physiol. 29
    • Seibert, A. F., A. E. Taylor, J. B. Bass, and J. Haynes, Jr. Hemoglobin potentiates oxidant injury in isolated rat lungs. Am. J. Physiol. 260 (Heart Circ. Physiol. 29): H1980-H1984, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Seibert, A.F.1    Taylor, A.E.2    Bass, J.B.3    Haynes Jr., J.4
  • 57
    • 0016616098 scopus 로고
    • Electron spin resonance study on peroxidase- and oxidase- reactions of horseradish peroxidase and methemoglobin
    • Shiga, T., and K. Imaizumi. Electron spin resonance study on peroxidase- and oxidase- reactions of horseradish peroxidase and methemoglobin. Arch. Biochem. Biophys. 167: 469-479, 1975.
    • (1975) Arch. Biochem. Biophys. , vol.167 , pp. 469-479
    • Shiga, T.1    Imaizumi, K.2
  • 58
    • 0029052167 scopus 로고
    • Increased lipid peroxidation and decreased antioxidants in lungs of guinea pigs following an allergic pulmonary response
    • Shvedova, A. A., E. R. Kisin, V. E. Kagan, and M. N. Karol. Increased lipid peroxidation and decreased antioxidants in lungs of guinea pigs following an allergic pulmonary response. Toxicol. Appl. Pharmacol. 132: 72-81, 1995.
    • (1995) Toxicol. Appl. Pharmacol. , vol.132 , pp. 72-81
    • Shvedova, A.A.1    Kisin, E.R.2    Kagan, V.E.3    Karol, M.N.4
  • 60
    • 0027787910 scopus 로고
    • Tyrosinase-induced phenoxyl radicals of etoposide (VP-16): Interaction with reductants in model system, K 562 leukemic cell and nuclear homogenates
    • Stoyanovsky, D., J. Yalowich, T. Gantchev, and V. Kagan. Tyrosinase-induced phenoxyl radicals of etoposide (VP-16): interaction with reductants in model system, K 562 leukemic cell and nuclear homogenates. Free Radical Res. Commun. 19: 371-386, 1993.
    • (1993) Free Radical Res. Commun. , vol.19 , pp. 371-386
    • Stoyanovsky, D.1    Yalowich, J.2    Gantchev, T.3    Kagan, V.4
  • 61
    • 0029893338 scopus 로고    scopus 로고
    • Detection and characterization of the EPR-silent glutathionyl-DMPO adduct derived from redox-cycling of phenoxyl radicals in model systems and HL-60 cells
    • Stoyanovsky, D. A., R. Goldman, S. S. Jonnalagadda, B. W. Day, H. G. Claycamp, and V. E. Kagan. Detection and characterization of the EPR-silent glutathionyl-DMPO adduct derived from redox-cycling of phenoxyl radicals in model systems and HL-60 cells. Arch. Biochem. Biophys. 330: 3-11, 1996.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 3-11
    • Stoyanovsky, D.A.1    Goldman, R.2    Jonnalagadda, S.S.3    Day, B.W.4    Claycamp, H.G.5    Kagan, V.E.6
  • 62
    • 0038360739 scopus 로고
    • The physics and mechanisms of primary blast injury. Primary blast injury and basic research
    • edited by R. Bellamy and R. Zaitchuk. Washington, DC: Office of the Surgeon General, Department of the Army, USA
    • Stuhmiller, J. H., Y. Y. Phillips III, and D. R. Richmond. The physics and mechanisms of primary blast injury. Primary blast injury and basic research. In: Textbook of Military Medicine (Conventional Warfare, Ballistic, Blast, and Burn Injuries), edited by R. Bellamy and R. Zaitchuk. Washington, DC: Office of the Surgeon General, Department of the Army, USA, 1991, vol. 5, p. 221-270.
    • (1991) Textbook of Military Medicine (Conventional Warfare, Ballistic, Blast, and Burn Injuries) , vol.5 , pp. 221-270
    • Stuhmiller, J.H.1    Phillips III, Y.Y.2    Richmond, D.R.3
  • 63
    • 0023317551 scopus 로고
    • Oxidants and antioxidants in the lung
    • Travis, J. Oxidants and antioxidants in the lung. Am. Rev. Respir. Dis. 135: 773-774, 1987.
    • (1987) Am. Rev. Respir. Dis. , vol.135 , pp. 773-774
    • Travis, J.1
  • 64
    • 0016719298 scopus 로고
    • Fractionation and analysis of fluorescent products of lipid peroxidation
    • Trombly, R., and A. Tappel. Fractionation and analysis of fluorescent products of lipid peroxidation. Lipids 10: 441-447, 1975.
    • (1975) Lipids , vol.10 , pp. 441-447
    • Trombly, R.1    Tappel, A.2
  • 65
    • 0002720711 scopus 로고
    • Effects of oxidants and antioxidants evaluated using parinaric acid as a sensitive probe for oxidative stress
    • Van den Berg, J. J. M. Effects of oxidants and antioxidants evaluated using parinaric acid as a sensitive probe for oxidative stress. Redox Reports 1: 11-21, 1994.
    • (1994) Redox Reports , vol.1 , pp. 11-21
    • Van Den Berg, J.J.M.1
  • 66
    • 0030031737 scopus 로고    scopus 로고
    • ESR spin trapping investigation of radical formation from the reaction between hematin and tert-butyl hydroperoxide
    • Van der Zee, J., D. P. Barr, and R. P. Mason. ESR spin trapping investigation of radical formation from the reaction between hematin and tert-butyl hydroperoxide. Free Radical Biol. Med. 20: 199-206, 1996.
    • (1996) Free Radical Biol. Med. , vol.20 , pp. 199-206
    • Van Der Zee, J.1    Barr, D.P.2    Mason, R.P.3
  • 67
    • 0025145949 scopus 로고
    • Oxidative reactions of hemoglobin
    • Winterbourn, C. C. Oxidative reactions of hemoglobin. Methods Enzymol. 186: 265-272, 1990.
    • (1990) Methods Enzymol. , vol.186 , pp. 265-272
    • Winterbourn, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.