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Volumn , Issue , 2011, Pages 327-343

Detection of Reactive Metabolites of Oxygen and Nitrogen

Author keywords

Aconitase activity inhibition; Chemiluminescence probes; Chemiluminescent technique sensitivity; Detection of reactive metabolites of oxygen; Environmentally generated ros, organic ros and nox; Exogenous and endogenous sources of ros; Methods, quantifying major ros and nox; Myeloperoxidase (MPO); Oxidative stress detection methods; Peroxidase based assays and H2O2 generation

Indexed keywords


EID: 84886018364     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781444345988.ch24     Document Type: Chapter
Times cited : (8)

References (98)
  • 1
    • 74049100448 scopus 로고    scopus 로고
    • Reactive photoinduced species in estuarinewaters. Characterization of hydroxyl radical, singlet oxygen and dissolved organic matter triplet state in natural oxidation processes
    • Al Housari, F., Vione, D., Chiron, S., Barbati, S. 2010 Reactive photoinduced species in estuarinewaters. Characterization of hydroxyl radical, singlet oxygen and dissolved organic matter triplet state in natural oxidation processes. Photochemistry and Photobiology Science 9, 78-86.
    • (2010) Photochemistry and Photobiology Science , vol.9 , pp. 78-86
    • Al Housari, F.1    Vione, D.2    Chiron, S.3    Barbati, S.4
  • 2
    • 70350005373 scopus 로고    scopus 로고
    • Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation
    • Allen, B.W., Stamler, J.S., Piantadosi, C.A. 2009 Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation. Trends in MolecularMedicine 15, 452-460.
    • (2009) Trends in Molecular Medicine , vol.15 , pp. 452-460
    • Allen, B.W.1    Stamler, J.S.2    Piantadosi, C.A.3
  • 3
    • 0016689082 scopus 로고
    • The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes
    • Azzi, A., Montecucco, C., Richter, C. 1975 The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes. Biochemical and Biophysical Research Communications 65, 597-603.
    • (1975) Biochemical and Biophysical Research Communications , vol.65 , pp. 597-603
    • Azzi, A.1    Montecucco, C.2    Richter, C.3
  • 4
    • 0034281968 scopus 로고    scopus 로고
    • Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques
    • Barbacanne, M.A., Souchard, J.P., Darblade, B. et al. 2000 Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques. Free Radical Biology andMedicine 29, 388-396.
    • (2000) Free Radical Biology andMedicine , vol.29 , pp. 388-396
    • Barbacanne, M.A.1    Souchard, J.P.2    Darblade, B.3
  • 5
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
    • Beckman, J.S., Koppenol, W.H. 1996 Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. American Journal of Physiology 271, C1424-C1437.
    • (1996) American Journal of Physiology , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 6
    • 0032211437 scopus 로고    scopus 로고
    • Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical
    • Benov, L., Sztejnberg, L., Fridovich, I. 1998 Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical. Free Radical Biology and Medicine 25, 826-831.
    • (1998) Free Radical Biology and Medicine , vol.25 , pp. 826-831
    • Benov, L.1    Sztejnberg, L.2    Fridovich, I.3
  • 7
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine
    • Bindokas, V.P., Jordan, J., Lee, C.C.,Miller, R.J. 1996 Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine. Journal of Neuroscience 16, 1324-1336.
    • (1996) Journal of Neuroscience , vol.16 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 8
    • 33644872102 scopus 로고    scopus 로고
    • The oxidation of 2',7'-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy?
    • Bonini, M.G., Rota, C., Tomasi, A., Mason, R.P. (2006) The oxidation of 2',7'-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy? Free Radical Biology and Medicine 40, 968-975.
    • (2006) Free Radical Biology and Medicine , vol.40 , pp. 968-975
    • Bonini, M.G.1    Rota, C.2    Tomasi, A.3    Mason, R.P.4
  • 9
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris, A. 1984 Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Methods in Enzymology 105, 429-435.
    • (1984) Methods in Enzymology , vol.105 , pp. 429-435
    • Boveris, A.1
  • 10
    • 0017407172 scopus 로고
    • Evaluation of the horseradish peroxidase-scopoletin method for the measurement of hydrogen peroxide formation in biological systems
    • Boveris, A., Martino, E., Stoppani, A.O. 1977 Evaluation of the horseradish peroxidase-scopoletin method for the measurement of hydrogen peroxide formation in biological systems. Annals of Biochemistry 80, 145-158.
    • (1977) Annals of Biochemistry , vol.80 , pp. 145-158
    • Boveris, A.1    Martino, E.2    Stoppani, A.O.3
  • 11
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan, M.L., Wu, W., Fu, X. et al. 2002 A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. Journal of Biological Chemistry, 277, 17415-17427.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3
  • 12
    • 34547093890 scopus 로고    scopus 로고
    • Methods to detect nitric oxide and its metabolites in biological samples
    • Bryan, N.S., Grisham, M.B. 2007 Methods to detect nitric oxide and its metabolites in biological samples. Free Radical Biology and Medicine 43, 645-657.
    • (2007) Free Radical Biology and Medicine , vol.43 , pp. 645-657
    • Bryan, N.S.1    Grisham, M.B.2
  • 13
    • 0030761155 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells
    • Budd, S.L., Castilho, R.F., Nicholls, D.G.(1997)Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells. FEBS Letters 415, 21-24.
    • (1997) FEBS Letters , vol.415 , pp. 21-24
    • Budd, S.L.1    Castilho, R.F.2    Nicholls, D.G.3
  • 14
    • 0028369668 scopus 로고
    • Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells
    • Carter,W.O.,Narayanan,P.K., Robinson, J.P. (1994)Intracellular hydrogen peroxide and superoxide anion detection in endothelial cells. Journal of Leukocyte Biology 55, 253-258.
    • (1994) Journal of Leukocyte Biology , vol.55 , pp. 253-258
    • Carter, W.O.1    Narayanan, P.K.2    Robinson, J.P.3
  • 15
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro, L., Rodriguez,M., Radi, R. 1994 Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. Journal of Biological Chemistry 269, 29409-29415.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 16
    • 0021027358 scopus 로고
    • Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay
    • Cathcart, R., Schwiers, E., Ames, B.N. 1983 Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Analytical Biochemistry 134, 111-116.
    • (1983) Analytical Biochemistry , vol.134 , pp. 111-116
    • Cathcart, R.1    Schwiers, E.2    Ames, B.N.3
  • 17
    • 0030200706 scopus 로고    scopus 로고
    • A modified catalase assay suitable for a plate reader and for the analysis of brain cell cultures
    • Cohen, G., Kim, M., Ogwu, V. 1996 A modified catalase assay suitable for a plate reader and for the analysis of brain cell cultures. Journal of Neuroscience Methods 67, 53-56.
    • (1996) Journal of Neuroscience Methods , vol.67 , pp. 53-56
    • Cohen, G.1    Kim, M.2    Ogwu, V.3
  • 18
    • 0031423791 scopus 로고    scopus 로고
    • Dichlorodihydrofluorescein and dihydrorhodamine 123 are sensitive indicators of peroxynitrite in vitro: implications for intracellularmeasurement of reactive nitrogen and oxygen species
    • Crow, J.P. 1997 Dichlorodihydrofluorescein and dihydrorhodamine 123 are sensitive indicators of peroxynitrite in vitro: implications for intracellularmeasurement of reactive nitrogen and oxygen species. Nitric Oxide 1, 145-157.
    • (1997) Nitric Oxide , vol.1 , pp. 145-157
    • Crow, J.P.1
  • 20
    • 0029760021 scopus 로고    scopus 로고
    • Formation of nitrating and chlorinating speciesbyreaction ofnitritewithhypochlorousacid.Anovel mechanism for nitric oxide-mediated protein modification
    • Eiserich, J.P., Cross, C.E., Jones, A.D., Halliwell, B., van der Vliet, A. 1996 Formation of nitrating and chlorinating speciesbyreaction ofnitritewithhypochlorousacid.Anovel mechanism for nitric oxide-mediated protein modification. Journal of Biological Chemistry, 271, 19199-19208.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 19199-19208
    • Eiserich, J.P.1    Cross, C.E.2    Jones, A.D.3    Halliwell, B.4    van der Vliet, A.5
  • 21
    • 0037189377 scopus 로고    scopus 로고
    • Myeloperoxidase, a leukocyte-derived vascular NO oxidase
    • Eiserich, J.P., Baldus, S., Brennan,M.L. et al. (2002) Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science 296, 2391-2394.
    • (2002) Science , vol.296 , pp. 2391-2394
    • Eiserich, J.P.1    Baldus, S.2    Brennan, M.L.3
  • 22
    • 0035839611 scopus 로고    scopus 로고
    • Distinction between nitrosatingmechanisms within human cells and aqueous solution
    • Espey, M.G., Miranda, K.M., Thomas, D.D., Wink, D.A. 2001 Distinction between nitrosatingmechanisms within human cells and aqueous solution. Journal of Biological Chemistry 276, 30085-30091.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 30085-30091
    • Espey, M.G.1    Miranda, K.M.2    Thomas, D.D.3    Wink, D.A.4
  • 24
    • 0037143608 scopus 로고    scopus 로고
    • Focusing of nitric oxide mediated nitrosation and oxidative nitrosylation as a consequence of reaction with superoxide
    • USA
    • Espey, M.G., Thomas, D.D., Miranda, K.M., Wink, D.A. (2002b) Focusing of nitric oxide mediated nitrosation and oxidative nitrosylation as a consequence of reaction with superoxide. Proceedings of the National Academy of Sciences USA 99, 11127-11132.
    • (2002) Proceedings of the National Academy of Sciences , vol.99 , pp. 11127-11132
    • Espey, M.G.1    Thomas, D.D.2    Miranda, K.M.3    Wink, D.A.4
  • 25
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D.H., Tuminello, J.F., Emptage, M.H. 1993 The inactivation of Fe-S cluster containing hydro-lyases by superoxide. Journal of Biological Chemistry 268, 22369-22376.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 28
    • 85052768098 scopus 로고
    • Cytochrome c.
    • In Greenwald, R.A. (ed.)Handbook of Methods for Oxygen Radical Research. Raton, FL, CRC Press
    • Fridovich, I. (1985) Cytochrome c. In Greenwald, R.A. (ed.)Handbook of Methods for Oxygen Radical Research. Raton, FL, CRC Press, pp. 121-122.
    • (1985) , pp. 121-122
    • Fridovich, I.1
  • 31
    • 0030050838 scopus 로고    scopus 로고
    • Superoxide scavenging by Mn(II/III) tetrakis (1-methyl-4-pyridyl) porphyrin in mammalian cells
    • Gardner, P.R., Nguyen, D.D., White, C.W. 1996 Superoxide scavenging by Mn(II/III) tetrakis (1-methyl-4-pyridyl) porphyrin in mammalian cells. Archives of Biochemistry and Biophysics 325, 20-28.
    • (1996) Archives of Biochemistry and Biophysics , vol.325 , pp. 20-28
    • Gardner, P.R.1    Nguyen, D.D.2    White, C.W.3
  • 33
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R., Reed, J.C. 1998 Mitochondria and apoptosis. Science 281, 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 36
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen, A., Fridovich, I. 1994 Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. Journal of Biological Chemistry 269, 29405-29408.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 37
    • 0029819752 scopus 로고    scopus 로고
    • Measuring nitric oxide and superoxide: rate constants for aconitase reactivity
    • [Review] [19 refs]
    • Hausladen, A., Fridovich, I. 1996 Measuring nitric oxide and superoxide: rate constants for aconitase reactivity. [Review] [19 refs]. Methods in Enzymology 269, 37-41.
    • (1996) Methods in Enzymology , vol.269 , pp. 37-41
    • Hausladen, A.1    Fridovich, I.2
  • 38
    • 0035793616 scopus 로고    scopus 로고
    • Mechanismsunderlying endothelial dysfunction in diabetesmellitus
    • Hink,U., Li,H.,Mollnau,H. et al. (2001)Mechanismsunderlying endothelial dysfunction in diabetesmellitus. Circulation Research, 88, E14-E22.
    • (2001) Circulation Research , vol.88
    • Hink, U.1    Li, H.2    Mollnau, H.3
  • 40
    • 0021160336 scopus 로고
    • A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: its use in the simultaneous fluorimetric assay of cellular activation processes
    • Hyslop, P.A., Sklar, L.A. 1984 A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: its use in the simultaneous fluorimetric assay of cellular activation processes. Analytical Biochemistry 141, 280-286.
    • (1984) Analytical Biochemistry , vol.141 , pp. 280-286
    • Hyslop, P.A.1    Sklar, L.A.2
  • 41
    • 0027184205 scopus 로고
    • Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide from L-arginine
    • Ignarro, L.J., Fukuto, J.M., Griscavage, J.M., Rogers, N.E., Byrns, R.E. 1993 Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide from L-arginine. Proceedings of the National Academy of Sciences USA 90, 8103-8107.
    • (1993) Proceedings of the National Academy of Sciences USA , vol.90 , pp. 8103-8107
    • Ignarro, L.J.1    Fukuto, J.M.2    Griscavage, J.M.3    Rogers, N.E.4    Byrns, R.E.5
  • 42
    • 0030738911 scopus 로고    scopus 로고
    • Acceleration of oxidative stress-induced endothelial cell death by nitric oxide synthase dysfunction accompanied with decrease in tetrahydrobiopterin content
    • Ishii, M., Shimizu, S., Yamamoto, T., Momose, K., Kuroiwa, Y. 1997 Acceleration of oxidative stress-induced endothelial cell death by nitric oxide synthase dysfunction accompanied with decrease in tetrahydrobiopterin content. Life Sciences 61, 739-747.
    • (1997) Life Sciences , vol.61 , pp. 739-747
    • Ishii, M.1    Shimizu, S.2    Yamamoto, T.3    Momose, K.4    Kuroiwa, Y.5
  • 46
    • 0008247296 scopus 로고
    • The fluorometric analysis of ultramicro quantities of hydrogen peroxide
    • Keston, A.S., Brandt, R. 1965 The fluorometric analysis of ultramicro quantities of hydrogen peroxide. Annals of Biochemistry 11, 1-5.
    • (1965) Annals of Biochemistry , vol.11 , pp. 1-5
    • Keston, A.S.1    Brandt, R.2
  • 49
    • 0032109160 scopus 로고    scopus 로고
    • Detection and imaging of nitric oxide with novel fluorescent indicators: diaminofluoresceins
    • Kojima, H., Nakatsubo, N., Kikuchi, K. et al. (1998a) Detection and imaging of nitric oxide with novel fluorescent indicators: diaminofluoresceins. Analytical Chemistry 70, 2446-2453.
    • (1998) Analytical Chemistry , vol.70 , pp. 2446-2453
    • Kojima, H.1    Nakatsubo, N.2    Kikuchi, K.3
  • 50
    • 0031940489 scopus 로고    scopus 로고
    • Development of a fluorescent indicator for nitric oxide based on the fluorescein chromophore
    • Kojima, H., Sakurai, K., Kikuchi, K. et al. (1998b) Development of a fluorescent indicator for nitric oxide based on the fluorescein chromophore. Chemical and Pharmaceutical Bulletin 46, 373-375.
    • (1998) Chemical and Pharmaceutical Bulletin , vol.46 , pp. 373-375
    • Kojima, H.1    Sakurai, K.2    Kikuchi, K.3
  • 52
    • 0020320783 scopus 로고
    • Aquantitative test for superoxide radicals produced in biological systems
    • Kuthan,H., Ullrich, V., Estabrook, R.W. (1982)Aquantitative test for superoxide radicals produced in biological systems. Biochemical Journal 203, 551-558.
    • (1982) Biochemical Journal , vol.203 , pp. 551-558
    • Kuthan, H.1    Ullrich, V.2    Estabrook, R.W.3
  • 53
    • 0037399439 scopus 로고    scopus 로고
    • Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension
    • Landmesser, U., Dikalov, S., Price, S.R. et al. 2003 Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension. Journal of Clinical Investigation 111, 1201-1209.
    • (2003) Journal of Clinical Investigation , vol.111 , pp. 1201-1209
    • Landmesser, U.1    Dikalov, S.2    Price, S.R.3
  • 54
    • 0030068894 scopus 로고    scopus 로고
    • Peroxidativeoxidation of leuco-dichlorofluorescein by prostaglandin H synthase in prostaglandin biosynthesis from polyunsaturated fatty acids
    • Larsen, L.N.,Dahl, E.,Bremer, J. 1996 Peroxidativeoxidation of leuco-dichlorofluorescein by prostaglandin H synthase in prostaglandin biosynthesis from polyunsaturated fatty acids. Biochimica et Biophysica Acta 1299, 47-53.
    • (1996) Biochimica et Biophysica Acta , vol.1299 , pp. 47-53
    • Larsen, L.N.1    Dahl, E.2    Bremer, J.3
  • 55
    • 0026554428 scopus 로고
    • Evaluation of the probe 2',7'-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • LeBel, C.P., Ischiropoulos, H., Bondy, S.C. 1992 Evaluation of the probe 2',7'-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress. Chemistry Research in Toxicology 5, 227-231.
    • (1992) Chemistry Research in Toxicology , vol.5 , pp. 227-231
    • LeBel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 56
    • 33645220455 scopus 로고    scopus 로고
    • Oxidative stress inmarine environments: biochemistry and physiological ecology
    • Lesser,M.P. 2006 Oxidative stress inmarine environments: biochemistry and physiological ecology. Annual Review of Physiology 68, 253-278.
    • (2006) Annual Review of Physiology , vol.68 , pp. 253-278
    • Lesser, M.P.1
  • 57
    • 0030989642 scopus 로고    scopus 로고
    • Lucigenin (bis-Nmethylacridinium) as a mediator of superoxide anion production
    • Liochev, S.I., Fridovich, I. 1997 Lucigenin (bis-Nmethylacridinium) as a mediator of superoxide anion production. Archives of Biochemistry and Biophysics 337, 115-120.
    • (1997) Archives of Biochemistry and Biophysics , vol.337 , pp. 115-120
    • Liochev, S.I.1    Fridovich, I.2
  • 58
    • 0026492717 scopus 로고
    • Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils
    • Lucas, M., Solano, F. 1992 Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils. Analytical Biochemistry 206, 273-277.
    • (1992) Analytical Biochemistry , vol.206 , pp. 273-277
    • Lucas, M.1    Solano, F.2
  • 59
    • 0000474831 scopus 로고
    • Irreversible reaction of 3-amino 1, 2,4-triazole and related inhibitors with the protein catalase
    • Margoliash, E., Novogrodsky, A., Schejter, A. 1960 Irreversible reaction of 3-amino 1, 2,4-triazole and related inhibitors with the protein catalase. Biochemical Journal 74, 339-348.
    • (1960) Biochemical Journal , vol.74 , pp. 339-348
    • Margoliash, E.1    Novogrodsky, A.2    Schejter, A.3
  • 60
    • 0021288848 scopus 로고
    • Measurement of O-2 production by human neutrophils. The preparation and assay of NADPH oxidase-containing particles from human neutrophils
    • Markert, M., Andrews, P.C., Babior, B.M. (1984) Measurement of O-2 production by human neutrophils. The preparation and assay of NADPH oxidase-containing particles from human neutrophils. Methods in Enzymology 105, 358-365.
    • (1984) Methods in Enzymology , vol.105 , pp. 358-365
    • Markert, M.1    Andrews, P.C.2    Babior, B.M.3
  • 61
    • 49749184695 scopus 로고
    • The microestimation of succinate and the extinction coefficient of cytochrome c
    • Massey, V. 1959 The microestimation of succinate and the extinction coefficient of cytochrome c. Biochimica et Biophysica Acta 34, 255-256.
    • (1959) Biochimica et Biophysica Acta , vol.34 , pp. 255-256
    • Massey, V.1
  • 63
    • 0029799950 scopus 로고    scopus 로고
    • Determination of nitric oxide using fluorescence spectroscopy
    • Miles, A.M., Wink, D.A., Cook, J.C., Grisham, M.B. 1996 Determination of nitric oxide using fluorescence spectroscopy. Methods in Enzymology 268, 105-120.
    • (1996) Methods in Enzymology , vol.268 , pp. 105-120
    • Miles, A.M.1    Wink, D.A.2    Cook, J.C.3    Grisham, M.B.4
  • 64
    • 0344043305 scopus 로고    scopus 로고
    • Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis
    • Miller, F.J., Gutterman, D.D., Rios, C.D., Heistad, D.D., Davidson, B.L. 1998 Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis. Circulation Research 82, 1298-1305.
    • (1998) Circulation Research , vol.82 , pp. 1298-1305
    • Miller, F.J.1    Gutterman, D.D.2    Rios, C.D.3    Heistad, D.D.4    Davidson, B.L.5
  • 66
    • 0025033425 scopus 로고
    • Assay for superoxide dismutase based on chemiluminescence of luciferin analog
    • Nakano, M. (1990a) Assay for superoxide dismutase based on chemiluminescence of luciferin analog. Methods in Enzymology 186, 227-232.
    • (1990) Methods in Enzymology , vol.186 , pp. 227-232
    • Nakano, M.1
  • 67
    • 0025075792 scopus 로고
    • Determination of superoxide radical and singlet oxygen based on chemiluminescence of luciferin analogs
    • Nakano, M. (1990b) Determination of superoxide radical and singlet oxygen based on chemiluminescence of luciferin analogs. Methods in Enzymology 186, 585-591.
    • (1990) Methods in Enzymology , vol.186 , pp. 585-591
    • Nakano, M.1
  • 68
    • 0029840829 scopus 로고    scopus 로고
    • Colorimetric assays for nitric oxide and nitrogen oxide species formed from nitric oxide stock solutions and donor compounds
    • Nims, R.W., Cook, J.C.,Krishna, M.C. et al. (1996) Colorimetric assays for nitric oxide and nitrogen oxide species formed from nitric oxide stock solutions and donor compounds. Methods in Enzymology 268, 93-105.
    • (1996) Methods in Enzymology , vol.268 , pp. 93-105
    • Nims, R.W.1    Cook, J.C.2    Krishna, M.C.3
  • 69
    • 0021288849 scopus 로고
    • Superoxide production
    • O'Brien, P.J. 1984 Superoxide production. Methods in Enzymology 105, 370-378.
    • (1984) Methods in Enzymology , vol.105 , pp. 370-378
    • O'Brien, P.J.1
  • 71
    • 26644457183 scopus 로고    scopus 로고
    • Nitric oxide in marine invertebrates: a comparative perspective
    • Palumbo, A. 2005 Nitric oxide in marine invertebrates: a comparative perspective. Comparative Biochemistry and Physiology A 142, 241-248.
    • (2005) Comparative Biochemistry and Physiology A , vol.142 , pp. 241-248
    • Palumbo, A.1
  • 72
    • 0025572711 scopus 로고
    • Regional H2O2 concentration in rat brain after hyperoxic convulsions
    • Piantadosi, C.A., Tatro, L.G. 1990 Regional H2O2 concentration in rat brain after hyperoxic convulsions. Journal of Applied Physiology 69, 1761-1766.
    • (1990) Journal of Applied Physiology , vol.69 , pp. 1761-1766
    • Piantadosi, C.A.1    Tatro, L.G.2
  • 73
    • 0019140628 scopus 로고
    • A simple colorimetric method for themeasurement of hydrogen peroxide produced by cells in culture
    • Pick, E., Keisari, Y. 1980 A simple colorimetric method for themeasurement of hydrogen peroxide produced by cells in culture. Journal of ImmunologicalMethods 38, 161-170.
    • (1980) Journal of ImmunologicalMethods , vol.38 , pp. 161-170
    • Pick, E.1    Keisari, Y.2
  • 75
    • 0032830132 scopus 로고    scopus 로고
    • Evidence for free radical formation during the oxidation of 2'-7'-dichlorofluorescin to the fluorescent dye 2'-7'-dichlorofluorescein by horseradish peroxidase: possible implications for oxidative stress measurements
    • Rota, C., Chignell, C.F., Mason, R.P. 1999 Evidence for free radical formation during the oxidation of 2'-7'-dichlorofluorescin to the fluorescent dye 2'-7'-dichlorofluorescein by horseradish peroxidase: possible implications for oxidative stress measurements. Free Radical Biology and Medicine 27, 873-881.
    • (1999) Free Radical Biology and Medicine , vol.27 , pp. 873-881
    • Rota, C.1    Chignell, C.F.2    Mason, R.P.3
  • 76
    • 0027249757 scopus 로고
    • Evaluation of 2',7'-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells
    • Royall, J.A., Ischiropoulos, H. 1993 Evaluation of 2',7'-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells. Archives of Biochemistry and Biophysics 302, 348-355.
    • (1993) Archives of Biochemistry and Biophysics , vol.302 , pp. 348-355
    • Royall, J.A.1    Ischiropoulos, H.2
  • 77
    • 0020642791 scopus 로고
    • Assay of H2O2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase
    • Ruch, W., Cooper, P.H., Baggiolini, M. 1983 Assay of H2O2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase. Journal of ImmunologicalMethods 63, 347-357.
    • (1983) Journal of ImmunologicalMethods , vol.63 , pp. 347-357
    • Ruch, W.1    Cooper, P.H.2    Baggiolini, M.3
  • 79
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • Saville, B. 1958 A scheme for the colorimetric determination of microgram amounts of thiols. Analyst 83, 670-672.
    • (1958) Analyst , vol.83 , pp. 670-672
    • Saville, B.1
  • 80
    • 0032551721 scopus 로고    scopus 로고
    • Quantification of superoxide radical formation in intact vascular tissue using a cypridina luciferin analog as an alternative to lucigenin
    • Skatchkov,M.P., Sperling, D.,Hink, U.,Anggard, E.,Munzel,T. 1998 Quantification of superoxide radical formation in intact vascular tissue using a cypridina luciferin analog as an alternative to lucigenin. Biochemical and Biophysical Research Communications 248, 382-386.
    • (1998) Biochemical and Biophysical Research Communications , vol.248 , pp. 382-386
    • Skatchkov, M.P.1    Sperling, D.2    Hink, U.3    Anggard, E.4    Munzel, T.5
  • 81
    • 0033582254 scopus 로고    scopus 로고
    • Validation of lucigenin as a chemiluminescent probe to monitor vascular superoxide as well as basal vascular nitric oxide production
    • Skatchkov, M.P., Sperling, D., Hink, U. et al. 1999 Validation of lucigenin as a chemiluminescent probe to monitor vascular superoxide as well as basal vascular nitric oxide production. Biochemical and Biophysical Research Communications 254, 319-324.
    • (1999) Biochemical and Biophysical Research Communications , vol.254 , pp. 319-324
    • Skatchkov, M.P.1    Sperling, D.2    Hink, U.3
  • 82
    • 0032834347 scopus 로고    scopus 로고
    • H(2)O(2) detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system
    • Staniek, K., Nohl, H. 1999 H(2)O(2) detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system. Biochimica et Biophysica Acta 1413, 70-80.
    • (1999) Biochimica et Biophysica Acta , vol.1413 , pp. 70-80
    • Staniek, K.1    Nohl, H.2
  • 84
    • 0035800889 scopus 로고    scopus 로고
    • Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite
    • Tarpey, M.M., Fridovich, I. 2001 Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite. Circulation Research 89, 224-236.
    • (2001) Circulation Research , vol.89 , pp. 224-236
    • Tarpey, M.M.1    Fridovich, I.2
  • 85
    • 0033612185 scopus 로고    scopus 로고
    • Chemiluminescent detection of oxidants in vascular tissue: lucigenin but not coelenterazine enhances superoxide formation
    • Tarpey,M.M.,White, C.R., Suarez, E.,Richardson, G.,Radi,R., Freeman, B.A. 1999 Chemiluminescent detection of oxidants in vascular tissue: lucigenin but not coelenterazine enhances superoxide formation. Circulation Research 84, 1203-1211.
    • (1999) Circulation Research , vol.84 , pp. 1203-1211
    • Tarpey, M.M.1    White, C.R.2    Suarez, E.3    Richardson, G.4    Radi, R.5    Freeman, B.A.6
  • 86
    • 1342289237 scopus 로고    scopus 로고
    • Methods for detection of reactive metabolites of oxygen and nitrogen: in vitro and in vivo considerations
    • Tarpey, M.M., Wink, D.A., Grisham, M.B. 2004 Methods for detection of reactive metabolites of oxygen and nitrogen: in vitro and in vivo considerations. American Journal of Physiology 286, R431-R444.
    • (2004) American Journal of Physiology , vol.286
    • Tarpey, M.M.1    Wink, D.A.2    Grisham, M.B.3
  • 87
    • 0031570749 scopus 로고    scopus 로고
    • Coelenterazine analogs as chemiluminescent probe for superoxide anion
    • Teranishi, K., Shimomura, O. 1997 Coelenterazine analogs as chemiluminescent probe for superoxide anion. Analytical Biochemistry 249, 37-43.
    • (1997) Analytical Biochemistry , vol.249 , pp. 37-43
    • Teranishi, K.1    Shimomura, O.2
  • 88
  • 89
    • 0028977904 scopus 로고
    • 2+oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems
    • Thomson, L., Trujillo, M., Telleri, R., Radi, R. (1995) Kinetics of cytochrome c2+oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems. Archives of Biochemistry and Biophysics 319, 491-497.
    • (1995) Archives of Biochemistry and Biophysics , vol.319 , pp. 491-497
    • Thomson, L.1    Trujillo, M.2    Telleri, R.3    Radi, R.4
  • 90
    • 0027426028 scopus 로고
    • The first application of a chemiluminescence probe, 2-methyl-6-[p-methoxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-3-one (MCLA), for detecting O-2 production, in vitro, from Kupffer cells stimulated by phorbol myristate acetate
    • Uehara, K., Maruyama, N., Huang, C.K., Nakano, M. 1993 The first application of a chemiluminescence probe, 2-methyl-6-[p-methoxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-3-one (MCLA), for detecting O-2 production, in vitro, from Kupffer cells stimulated by phorbol myristate acetate. FEBS Letters 335, 167-170.
    • (1993) FEBS Letters , vol.335 , pp. 167-170
    • Uehara, K.1    Maruyama, N.2    Huang, C.K.3    Nakano, M.4
  • 91
    • 0030962051 scopus 로고    scopus 로고
    • Continuous detection of superoxide in situ during ischemia and reperfusion in the rabbit heart
    • Ushiroda, S., Maruyama, Y., Nakano, M. 1997 Continuous detection of superoxide in situ during ischemia and reperfusion in the rabbit heart. Japanese Heart Journal 38, 91-105.
    • (1997) Japanese Heart Journal , vol.38 , pp. 91-105
    • Ushiroda, S.1    Maruyama, Y.2    Nakano, M.3
  • 92
    • 0242502758 scopus 로고    scopus 로고
    • Superoxide anion formationfrom lucigenin: an electron spin resonance spin-trapping study
    • Vasquez-Vivar, J., Hogg, N., Pritchard, K.A., Jr., Martasek, P., Kalyanaraman, B. (1997)Superoxide anion formationfrom lucigenin: an electron spin resonance spin-trapping study. FEBS Letters 403, 127-130.
    • (1997) FEBS Letters , vol.403 , pp. 127-130
    • Vasquez-vivar, J.1    Hogg, N.2    Pritchard Jr, K.A.3    Martasek, P.4    Kalyanaraman, B.5
  • 93
    • 0031740459 scopus 로고    scopus 로고
    • Detection of S-nitrosothiols by fluorometric and colorimetric methods
    • Wink, D.A., Kim, S., Coffin, D. et al. 1999 Detection of S-nitrosothiols by fluorometric and colorimetric methods. Methods in Enzymology 301, 201-211.
    • (1999) Methods in Enzymology , vol.301 , pp. 201-211
    • Wink, D.A.1    Kim, S.2    Coffin, D.3
  • 95
    • 0013142020 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescentproduct that is distinctly different fromethidium
    • Zhao, H.,Kalivendi, S.V., Joseph, J.,Zhang, H.,Kalyanaraman, B. 2002 Superoxide reacts with hydroethidine but forms a fluorescentproduct that is distinctly different fromethidium. Free Radical Biology and Medicine 33, S425.
    • (2002) Free Radical Biology and Medicine , vol.33
    • Zhao, H.1    Kalivendi, S.V.2    Joseph, J.3    Zhang, H.4    Kalyanaraman, B.5
  • 96
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou, M., Diwu, Z., Panchuk-Voloshina, N., Haugland, R.P. 1997 A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Analytical Biochemistry 253, 162-168.
    • (1997) Analytical Biochemistry , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-voloshina, N.3    Haugland, R.P.4
  • 98
    • 58149168842 scopus 로고    scopus 로고
    • HPLC study of oxidation products of hydroethidine in chemical and biological systems: ramifications in superoxide measurements
    • Zielonka, J., Hardy, M., Kalyanaraman, B. 2009 HPLC study of oxidation products of hydroethidine in chemical and biological systems: ramifications in superoxide measurements. Free Radical Biology and Medicine 46, 329-338.
    • (2009) Free Radical Biology and Medicine , vol.46 , pp. 329-338
    • Zielonka, J.1    Hardy, M.2    Kalyanaraman, B.3


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