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Volumn 21, Issue 3, 2016, Pages 208-217

Spectrophotometric assays for measuring redox biomarkers in blood

Author keywords

Antioxidants; biomarkers; blood; oxidative stress; spectrophotometer

Indexed keywords

BLOOD; HUMAN; OXIDATION REDUCTION REACTION; SCIENTIST; METABOLISM; OXIDATIVE STRESS; PROCEDURES; SPECTROPHOTOMETRY;

EID: 84958037735     PISSN: 1354750X     EISSN: 13665804     Source Type: Journal    
DOI: 10.3109/1354750X.2015.1126648     Document Type: Review
Times cited : (58)

References (74)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. (1984). Catalase in vitro. Methods Enzymol 105: 121-6
    • (1984) Methods Enzymol , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 0000024078 scopus 로고
    • Catalase
    • Bergmeyer HU, ed. Weinheim: Verlag Chemie
    • Aebi H. (1974). Catalase. In: Bergmeyer HU., ed. Methods of enzymatic analysis. Vol. 2. Weinheim: Verlag Chemie, 673-8
    • (1974) Methods of Enzymatic Analysis , vol.2 , pp. 673-678
    • Aebi, H.1
  • 3
    • 0030455884 scopus 로고    scopus 로고
    • Selenium and glutathione peroxidase reference values in whole blood and plasma of a reference population living in Valencia, Spain
    • Alegría A, Barberá R, Clemente G, et al. (1996). Selenium and glutathione peroxidase reference values in whole blood and plasma of a reference population living in Valencia, Spain. J Trace Elem Med Biol 10: 223-8
    • (1996) J Trace Elem Med Biol , vol.10 , pp. 223-228
    • Alegría, A.1    Barberá, R.2    Clemente, G.3
  • 4
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidant-and radical-caused aging and cancer: A hypothesis
    • Ames BN, Cathcart R, Schwiers E, Hochstein P. (1981). Uric acid provides an antioxidant defense in humans against oxidant-and radical-caused aging and cancer: a hypothesis. Proc Natl Acad Sci USA 78: 6858-62
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 5
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson NL, Anderson NG. (2002). The human plasma proteome: history, character, and diagnostic prospects. Mol Cell Proteomics 1: 845-67
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 6
    • 0037036051 scopus 로고    scopus 로고
    • Oxidative stress in toadfish (Halobactrachus didactylus) cardiac muscle. Acute exposure to vanadate oligomers
    • Aureliano M, Joaquim N, Sousa A, et al. (2002). Oxidative stress in toadfish (Halobactrachus didactylus) cardiac muscle. Acute exposure to vanadate oligomers. J Inorg Biochem 90: 159-65
    • (2002) J Inorg Biochem , vol.90 , pp. 159-165
    • Aureliano, M.1    Joaquim, N.2    Sousa, A.3
  • 7
    • 0021953310 scopus 로고
    • Plasma glutathione S-transferase measurements after paracetamol overdose: Evidence for early hepatocellular damage
    • Beckett GJ, Chapman BJ, Dyson EH, Hayes JD. (1985). Plasma glutathione S-transferase measurements after paracetamol overdose: evidence for early hepatocellular damage. Gut 26: 26-31
    • (1985) Gut , vol.26 , pp. 26-31
    • Beckett, G.J.1    Chapman, B.J.2    Dyson, E.H.3    Hayes, J.D.4
  • 8
    • 34547093890 scopus 로고    scopus 로고
    • Methods to detect nitric oxide and its metabolites in biological samples
    • Bryan NS, Grisham MB. (2007). Methods to detect nitric oxide and its metabolites in biological samples. Free Radic Biol Med 43: 645-57
    • (2007) Free Radic Biol Med , vol.43 , pp. 645-657
    • Bryan, N.S.1    Grisham, M.B.2
  • 9
    • 0019808342 scopus 로고
    • Glutathione-S-transferase of human red blood cells; Assay, values in normal subjects and in two pathological circumstances: Hyperbilirubinemia and impaired renal function
    • Carmagnol F, Sinet PM, Rapin J, Jerome H. (1981). Glutathione-S-transferase of human red blood cells; assay, values in normal subjects and in two pathological circumstances: hyperbilirubinemia and impaired renal function. Clin Chim Acta 117: 209-17
    • (1981) Clin Chim Acta , vol.117 , pp. 209-217
    • Carmagnol, F.1    Sinet, P.M.2    Rapin, J.3    Jerome, H.4
  • 11
    • 33747173091 scopus 로고    scopus 로고
    • Protein carbonylation, cellular dysfunction, and disease progression
    • Dalle-Donne I, Aldini G, Carini M, et al. (2006). Protein carbonylation, cellular dysfunction, and disease progression. J Cell Mol Med 10: 389-406
    • (2006) J Cell Mol Med , vol.10 , pp. 389-406
    • Dalle-Donne, I.1    Aldini, G.2    Carini, M.3
  • 12
    • 0037363715 scopus 로고    scopus 로고
    • Protein carbonyl groups as biomarkers of oxidative stress
    • Dalle-Donne I, Rossi R, Giustarini D, et al. (2003). Protein carbonyl groups as biomarkers of oxidative stress. Clin Chim Acta 329: 23-38
    • (2003) Clin Chim Acta , vol.329 , pp. 23-38
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3
  • 13
    • 1842785867 scopus 로고    scopus 로고
    • EPR spin trapping of protein radicals
    • Davies MJ, Hawkins CL. (2004). EPR spin trapping of protein radicals. Free Radic Biol Med 36: 1072-86
    • (2004) Free Radic Biol Med , vol.36 , pp. 1072-1086
    • Davies, M.J.1    Hawkins, C.L.2
  • 14
    • 0020062504 scopus 로고
    • A candidate reference method for uric acid in serum. I. Optimization and evaluation
    • Duncan PH, Gochman N, Cooper T, et al. (1982). A candidate reference method for uric acid in serum. I. Optimization and evaluation. Clin Chem 28: 284
    • (1982) Clin Chem , vol.28 , pp. 284
    • Duncan, P.H.1    Gochman, N.2    Cooper, T.3
  • 15
    • 0026551683 scopus 로고
    • Changes in blood glutathione concentrations and in erythrocyte glutathione reductase and glutathione S-transferase activity after running training and after participation in contests
    • Evelo CT, Palmen NG, Artur Y, Janssen GM. (1982). Changes in blood glutathione concentrations and in erythrocyte glutathione reductase and glutathione S-transferase activity after running training and after participation in contests. Eur J Appl Physiol Occup Physiol 64: 354-8
    • (1982) Eur J Appl Physiol Occup Physiol , vol.64 , pp. 354-358
    • Evelo, C.T.1    Palmen, N.G.2    Artur, Y.3    Janssen, G.M.4
  • 16
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohé L, Günzler WA. (1984). Assays of glutathione peroxidase. Methods Enzymol 105: 114-21
    • (1984) Methods Enzymol , vol.105 , pp. 114-121
    • Flohé, L.1    Günzler, W.A.2
  • 17
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: Overview of its protective roles, measurement, and biosynthesis
    • Forman HJ, Zhang H, Rinna A. (2009). Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med 30: 1-12
    • (2009) Mol Aspects Med , vol.30 , pp. 1-12
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 18
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner PR, Raineri I, Epstein LB, White CW. (1995). Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 270: 13399-405
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 19
    • 10644290884 scopus 로고    scopus 로고
    • Adaptation of the Griess reaction for detection of nitrite in human plasma
    • Giustarini D, Dalle-Donne I, Colombo R, et al. (2004). Adaptation of the Griess reaction for detection of nitrite in human plasma. Free Radic Res 38: 1235-40
    • (2004) Free Radic Res , vol.38 , pp. 1235-1240
    • Giustarini, D.1    Dalle-Donne, I.2    Colombo, R.3
  • 20
    • 33750906064 scopus 로고    scopus 로고
    • Age-related influence on thiol, disulfide, and protein-mixed disulfide levels in human plasma
    • Giustarini D, Dalle-Donne I, Lorenzini S, et al. (2006). Age-related influence on thiol, disulfide, and protein-mixed disulfide levels in human plasma. J Gerontol a Biol Sci Med Sci 61: 1030-8
    • (2006) J Gerontol A Biol Sci Med Sci , vol.61 , pp. 1030-1038
    • Giustarini, D.1    Dalle-Donne, I.2    Lorenzini, S.3
  • 21
    • 44849133593 scopus 로고    scopus 로고
    • Nitrite and nitrate measurement by Griess reagent in human plasma: Evaluation of interferences and standardization
    • Giustarini D, Rossi R, Milzani A, Dalle-Donne I. (2008). Nitrite and nitrate measurement by Griess reagent in human plasma: evaluation of interferences and standardization. Methods Enzymol 440: 361-80
    • (2008) Methods Enzymol , vol.440 , pp. 361-380
    • Giustarini, D.1    Rossi, R.2    Milzani, A.3    Dalle-Donne, I.4
  • 22
    • 84883383166 scopus 로고    scopus 로고
    • Analysis of GSH and GSSG after derivatization with N-ethylmaleimide
    • Giustarini D, Dalle-Donne I, Milzani A, et al. (2013). Analysis of GSH and GSSG after derivatization with N-ethylmaleimide. Nat Protoc 8: 1660-9
    • (2013) Nat Protoc , vol.8 , pp. 1660-1669
    • Giustarini, D.1    Dalle-Donne, I.2    Milzani, A.3
  • 23
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith OW. (1980). Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal Biochem 106: 207-12
    • (1980) Anal Biochem , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 24
    • 0016287254 scopus 로고
    • An improved coupled test procedure for glutathione peroxidase (EC 1-11-1-9-) in blood
    • Günzler WA, Kremers H, Flohé L. (1974). An improved coupled test procedure for glutathione peroxidase (EC 1-11-1-9-) in blood. Z Klin Chem Klin Biochem 12: 444-8
    • (1974) Z Klin Chem Klin Biochem , vol.12 , pp. 444-448
    • Günzler, W.A.1    Kremers, H.2    Flohé, L.3
  • 25
    • 0026322413 scopus 로고
    • Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood
    • Guemouri L, Artur Y, Herbeth B, et al. (1991). Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood. Clin Chem 37: 1932-7
    • (1991) Clin Chem , vol.37 , pp. 1932-1937
    • Guemouri, L.1    Artur, Y.2    Herbeth, B.3
  • 26
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • Habig WH, Jakoby WB. (1981). Assays for differentiation of glutathione S-transferases. Methods Enzymol 77: 398-405
    • (1981) Methods Enzymol , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 29
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: How should you do it and what do the results mean?
    • Halliwell B, Whiteman M. (2004). Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean? Br J Pharmacol 142: 231-55.
    • (2004) Br J Pharmacol , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 31
    • 0017911441 scopus 로고
    • The glutathione S-transferases: A group of multifunctional detoxification proteins
    • Jakoby WB. (1978). The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv Enzymol Relat Areas Mol Biol 46: 383-414
    • (1978) Adv Enzymol Relat Areas Mol Biol , vol.46 , pp. 383-414
    • Jakoby, W.B.1
  • 32
    • 80053601061 scopus 로고    scopus 로고
    • Biomarkers of Oxidative Stress Study IV: Ozone exposure of rats and its effect on antioxidants in plasma and bronchoalveolar lavage fluid
    • Kadiiska MB, Hatch GE, Nyska A, et al. (2011). Biomarkers of Oxidative Stress Study IV: ozone exposure of rats and its effect on antioxidants in plasma and bronchoalveolar lavage fluid. Free Radic Biol Med 51: 1636-42
    • (2011) Free Radic Biol Med , vol.51 , pp. 1636-1642
    • Kadiiska, M.B.1    Hatch, G.E.2    Nyska, A.3
  • 33
    • 0025264362 scopus 로고
    • Action of biologically-relevant oxidizing species upon uric acid. Identification of uric acid oxidation products
    • Kaur H, Halliwell B. (1990). Action of biologically-relevant oxidizing species upon uric acid. Identification of uric acid oxidation products. Chem Biol Interact 73: 235-47
    • (1990) Chem Biol Interact , vol.73 , pp. 235-247
    • Kaur, H.1    Halliwell, B.2
  • 34
    • 0032899615 scopus 로고    scopus 로고
    • Nitric oxide metabolism and breakdown
    • Kelm M. (1999). Nitric oxide metabolism and breakdown. Biochim Biophys Acta 1411: 273-89
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 273-289
    • Kelm, M.1
  • 35
    • 0025102226 scopus 로고
    • Determination of carbonyl content in oxidatively modified proteins
    • Levine RL, Garland D, Oliver CN, et al. (1990). Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 186: 464-78
    • (1990) Methods Enzymol , vol.186 , pp. 464-478
    • Levine, R.L.1    Garland, D.2    Oliver, C.N.3
  • 36
    • 0032032535 scopus 로고    scopus 로고
    • Alpha-glutathione transferases in HCV-related chronic hepatitis: A new predictive index of response to interferon therapy?
    • Loguercio C, Caporaso N, Tuccillo C, et al. (1998). Alpha-glutathione transferases in HCV-related chronic hepatitis: a new predictive index of response to interferon therapy? J Hepatol 28: 390-5.
    • (1998) J Hepatol , vol.28 , pp. 390-395
    • Loguercio, C.1    Caporaso, N.2    Tuccillo, C.3
  • 37
    • 84934272557 scopus 로고    scopus 로고
    • Blood reflects tissue oxidative stress: A systematic review
    • Margaritelis NV, Veskoukis AS, Paschalis V, et al. (2015). Blood reflects tissue oxidative stress: a systematic review. Biomarkers 20: 97-108
    • (2015) Biomarkers , vol.20 , pp. 97-108
    • Margaritelis, N.V.1    Veskoukis, A.S.2    Paschalis, V.3
  • 38
    • 0022713698 scopus 로고
    • On the multiplicity of the enzyme catalase in mammalian liver
    • Masters C, Pegg M, Cranc D. (1986). On the multiplicity of the enzyme catalase in mammalian liver. Mol Cell Biochem 70: 113-20
    • (1986) Mol Cell Biochem , vol.70 , pp. 113-120
    • Masters, C.1    Pegg, M.2    Cranc, D.3
  • 39
    • 0024212517 scopus 로고    scopus 로고
    • Superoxide dismutase: The first twenty years (1968-1988)
    • Mccord JM, Fridovich I. (1998). Superoxide dismutase: the first twenty years (1968-1988). Free Radic Biol Med 5: 363-9
    • (1998) Free Radic Biol Med , vol.5 , pp. 363-369
    • McCord, J.M.1    Fridovich, I.2
  • 40
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • Mccord JM, Fridovich I. (1969). Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-55
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 41
    • 0016228060 scopus 로고
    • Glutathione, metabolism and function via the gamma-glutamyl cycle
    • Meister A. (1974). Glutathione, metabolism and function via the gamma-glutamyl cycle. Life Sci 15: 177-90
    • (1974) Life Sci , vol.15 , pp. 177-190
    • Meister, A.1
  • 42
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • Moncada S, Palmer RMJ, Higgs A. (1991). Nitric oxide: physiology, pathophysiology and pharmacology. Pharmacol Rev 43: 109-42
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, A.3
  • 43
    • 33747057698 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress in G6PD-deficient individuals
    • Nikolaidis MG, Jamurtas AZ, Paschalis V, et al. (2006). Exercise-induced oxidative stress in G6PD-deficient individuals. Med Sci Sports Exerc 38: 1443-50
    • (2006) Med Sci Sports Exerc , vol.38 , pp. 1443-1450
    • Nikolaidis, M.G.1    Jamurtas, A.Z.2    Paschalis, V.3
  • 44
    • 84861108632 scopus 로고    scopus 로고
    • Redox biology of exercise: An integrative and comparative consideration of some overlooked issues
    • Nikolaidis MG, Kyparos A, Spanou C, et al. (2012). Redox biology of exercise: an integrative and comparative consideration of some overlooked issues. J Exp Biol 215: 1615-25
    • (2012) J Exp Biol , vol.215 , pp. 1615-1625
    • Nikolaidis, M.G.1    Kyparos, A.2    Spanou, C.3
  • 45
    • 85124115219 scopus 로고    scopus 로고
    • Common questions and tentative answers on how to assess oxidative stress after antioxidant supplementation and exercise
    • Lamprecht M, ed. New York: CRC Press
    • Nikolaidis MG, Margaritelis NV, Paschalis V, et al. (2015). Common questions and tentative answers on how to assess oxidative stress after antioxidant supplementation and exercise. In: Lamprecht M., ed. Antioxidants in sports nutrition. New York: CRC Press, 221-46
    • (2015) Antioxidants in Sports Nutrition , pp. 221-246
    • Nikolaidis, M.G.1    Margaritelis, N.V.2    Paschalis, V.3
  • 46
    • 0015592696 scopus 로고
    • The characteristics of the "e in ethanol oxidation" reaction of catalase in ethanol oxidation
    • Oshino N, Oshino R, Chance B. (1973). The characteristics of the "e in ethanol oxidation" reaction of catalase in ethanol oxidation. Biochem J 131: 555-67
    • (1973) Biochem J , vol.131 , pp. 555-567
    • Oshino, N.1    Oshino, R.2    Chance, B.3
  • 47
    • 1242314758 scopus 로고    scopus 로고
    • Thiol redox state (TRS) and oxidative stress in the mouse hippocampus after pentylenetetrazol-induced epileptic seizure
    • Patsoukis N, Zervoudakis G, Panagopoulos NT, et al. (2004). Thiol redox state (TRS) and oxidative stress in the mouse hippocampus after pentylenetetrazol-induced epileptic seizure. Neurosci Lett 357: 83-6
    • (2004) Neurosci Lett , vol.357 , pp. 83-86
    • Patsoukis, N.1    Zervoudakis, G.2    Panagopoulos, N.T.3
  • 48
    • 0019140628 scopus 로고
    • A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture
    • Pick E, Keisari Y. (1980). A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture. J Immunol Methods 38: 161-70
    • (1980) J Immunol Methods , vol.38 , pp. 161-170
    • Pick, E.1    Keisari, Y.2
  • 49
    • 84929152649 scopus 로고    scopus 로고
    • The role of antioxidants in the chemistry of oxidative stress: A review
    • Pisoschi AM, Pop A. (2015). The role of antioxidants in the chemistry of oxidative stress: a review. Eur J Med Chem 97: 55-74
    • (2015) Eur J Med Chem , vol.97 , pp. 55-74
    • Pisoschi, A.M.1    Pop, A.2
  • 50
    • 0017380842 scopus 로고
    • Glutathione peroxidase activity of glutathione-s-transferases purified from rat liver
    • Prohaska JR, Ganther HE. (1977). Glutathione peroxidase activity of glutathione-s-transferases purified from rat liver. Biochem Biophys Res Commun 76: 437-45
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 437-445
    • Prohaska, J.R.1    Ganther, H.E.2
  • 52
    • 0034681114 scopus 로고    scopus 로고
    • Modifications of proteins by polyunsaturated fatty acid peroxidation products
    • Refsgaard HH, Tsai L, Stadtman ER. (2000). Modifications of proteins by polyunsaturated fatty acid peroxidation products. Proc Natl Acad Sci USA 97: 611-16
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 611-616
    • Refsgaard, H.H.1    Tsai, L.2    Stadtman, E.R.3
  • 53
    • 0028239163 scopus 로고
    • Oxidative damage to proteins: Spectrophotometric method for carbonyl assay
    • Abelson NJ, Simon IM, eds. New York: Academic Press
    • Reznick ZA, Packer L. (1994). Oxidative damage to proteins: spectrophotometric method for carbonyl assay. In: Abelson NJ, Simon IM., eds. Methods in enzymology. Vol. 233. New York: Academic Press, 357-63
    • (1994) Methods in Enzymology , vol.233 , pp. 357-363
    • Reznick, Z.A.1    Packer, L.2
  • 54
    • 17644390613 scopus 로고    scopus 로고
    • Controlled elimination of intracellular H(2)O(2): Regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification
    • Rhee SG, Yang KS, Kang SW, et al. (2005). Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid Redox Signal 7: 619-26
    • (2005) Antioxid Redox Signal , vol.7 , pp. 619-626
    • Rhee, S.G.1    Yang, K.S.2    Kang, S.W.3
  • 55
    • 77955048966 scopus 로고    scopus 로고
    • Methods for detection and measurement of hydrogen peroxide inside and outside of cells
    • Rhee SG, Chang TS, Jeong W, Kang D. (2010). Methods for detection and measurement of hydrogen peroxide inside and outside of cells. Mol Cells 29: 539-49
    • (2010) Mol Cells , vol.29 , pp. 539-549
    • Rhee, S.G.1    Chang, T.S.2    Jeong, W.3    Kang, D.4
  • 56
    • 33745464371 scopus 로고    scopus 로고
    • Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress
    • Rossi R, Dalle-Donne I, Milzani A, Giustarini D. (2006). Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress. Clin Chem 52: 1406-14
    • (2006) Clin Chem , vol.52 , pp. 1406-1414
    • Rossi, R.1    Dalle-Donne, I.2    Milzani, A.3    Giustarini, D.4
  • 57
    • 0036231301 scopus 로고    scopus 로고
    • Blood glutathione disulfide: In vivo factor or in vitro artifact?
    • Rossi R, Milzani A, Dalle-Donne I, et al. (2002). Blood glutathione disulfide: in vivo factor or in vitro artifact? Clin Chem 48: 742-53.
    • (2002) Clin Chem , vol.48 , pp. 742-753
    • Rossi, R.1    Milzani, A.2    Dalle-Donne, I.3
  • 58
    • 0018842486 scopus 로고
    • Determination of uric acid with uricase and peroxidase
    • Sanders GT, Pasman AJ, Hoek FJ. (1980). Determination of uric acid with uricase and peroxidase. Clin Chim Acta 101: 299
    • (1980) Clin Chim Acta , vol.101 , pp. 299
    • Sanders, G.T.1    Pasman, A.J.2    Hoek, F.J.3
  • 59
    • 0034545361 scopus 로고    scopus 로고
    • Fully-automated spectrophotometric method for measurement of antioxidant activity of catalase
    • Slaughter MR, Obrien PJ. (2000). Fully-automated spectrophotometric method for measurement of antioxidant activity of catalase. Clin Biochem 33: 525-34
    • (2000) Clin Biochem , vol.33 , pp. 525-534
    • Slaughter, M.R.1    Obrien, P.J.2
  • 60
    • 0024199997 scopus 로고
    • Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid)
    • Smith IK, Vierheller TL, Thorne CA. (1988). Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis(2-nitrobenzoic acid). Anal Biochem 175: 408-13
    • (1988) Anal Biochem , vol.175 , pp. 408-413
    • Smith, I.K.1    Vierheller, T.L.2    Thorne, C.A.3
  • 61
    • 0020629019 scopus 로고
    • Antioxidant activity of uric acid and 3-N-ribosyluric acid with unsaturated fatty acids and erythrocyte membranes
    • Smith RC, Lawing L. (1983). Antioxidant activity of uric acid and 3-N-ribosyluric acid with unsaturated fatty acids and erythrocyte membranes. Arch Biochem Biophys 223: 166-72
    • (1983) Arch Biochem Biophys , vol.223 , pp. 166-172
    • Smith, R.C.1    Lawing, L.2
  • 62
    • 84856293321 scopus 로고    scopus 로고
    • The redox stress hypothesis of aging
    • Sohal RS, Orr WC. (2012). The redox stress hypothesis of aging. Free Radic Biol Med 52: 539-55
    • (2012) Free Radic Biol Med , vol.52 , pp. 539-555
    • Sohal, R.S.1    Orr, W.C.2
  • 63
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman ER. (1990). Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 9: 315-25
    • (1990) Free Radic Biol Med , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 64
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. (1993). Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 62: 797-821
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 65
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F. (1969). Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 27: 502-22
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 66
    • 34248140674 scopus 로고    scopus 로고
    • Analysis of nitrite and nitrate in biological fluids by assays based on the Griess reaction: Appraisal of the Griess reaction in the L-arginine/nitric oxide area of research
    • Tsikas D. (2007). Analysis of nitrite and nitrate in biological fluids by assays based on the Griess reaction: appraisal of the Griess reaction in the L-arginine/nitric oxide area of research. J Chromatogr B Analyt Technol Biomed Life Sci 851: 51-70
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.851 , pp. 51-70
    • Tsikas, D.1
  • 67
    • 22144457461 scopus 로고    scopus 로고
    • Methods of quantitative analysis of the nitric oxide metabolites nitrite and nitrate in human biological fluids
    • Tsikas D. (2005). Methods of quantitative analysis of the nitric oxide metabolites nitrite and nitrate in human biological fluids. Free Radic Res 39: 797-815
    • (2005) Free Radic Res , vol.39 , pp. 797-815
    • Tsikas, D.1
  • 68
    • 33749986298 scopus 로고    scopus 로고
    • Free radicals and antioxidants in normal physiological functions and human disease
    • Valko M, Leibfritz D, Monco J, et al. (2007). Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 39: 44-84
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 44-84
    • Valko, M.1    Leibfritz, D.2    Monco, J.3
  • 69
    • 57649178169 scopus 로고    scopus 로고
    • Effects of xanthine oxidase inhibition on oxidative stress and swimming performance in rats
    • Veskoukis AS, Nikolaidis MG, Kyparos A, et al. (2008). Effects of xanthine oxidase inhibition on oxidative stress and swimming performance in rats. Appl Physiol Nutr Metab 33: 1140-54
    • (2008) Appl Physiol Nutr Metab , vol.33 , pp. 1140-1154
    • Veskoukis, A.S.1    Nikolaidis, M.G.2    Kyparos, A.3
  • 70
    • 70350128251 scopus 로고    scopus 로고
    • Blood reflects tissue oxidative stress depending on biomarker and tissue studied
    • Veskoukis AS, Nikolaidis MG, Kyparos A, Kouretas D. (2009). Blood reflects tissue oxidative stress depending on biomarker and tissue studied. Free Radic Biol Med 47: 1371-4
    • (2009) Free Radic Biol Med , vol.47 , pp. 1371-1374
    • Veskoukis, A.S.1    Nikolaidis, M.G.2    Kyparos, A.3    Kouretas, D.4
  • 71
    • 84924119180 scopus 로고    scopus 로고
    • Are free radicals involved in thiol-based redox signaling?
    • Winterbourn CC. (2015). Are free radicals involved in thiol-based redox signaling? Free Radic Biol Med 80: 164-70
    • (2015) Free Radic Biol Med , vol.80 , pp. 164-170
    • Winterbourn, C.C.1
  • 72
    • 84880277784 scopus 로고    scopus 로고
    • The biological chemistry of hydrogen peroxide
    • Winterbourn CC. (2013). The biological chemistry of hydrogen peroxide. Methods Enzymol 528: 3-25
    • (2013) Methods Enzymol , vol.528 , pp. 3-25
    • Winterbourn, C.C.1
  • 73
    • 4344648152 scopus 로고    scopus 로고
    • Biomarkers of antioxidant capacity in the hydrophilic and lipophilic compartments of human plasma
    • Yeum KJ, Russell RM, Krinsky NI, Aldini G. (2004). Biomarkers of antioxidant capacity in the hydrophilic and lipophilic compartments of human plasma. Arch Biochem Biophys 430: 97-103
    • (2004) Arch Biochem Biophys , vol.430 , pp. 97-103
    • Yeum, K.J.1    Russell, R.M.2    Krinsky, N.I.3    Aldini, G.4
  • 74
    • 58149472199 scopus 로고    scopus 로고
    • Uricase based methods for determination of uric acid in serum
    • Zhao Y, Yang X, Lu W. (2009). Uricase based methods for determination of uric acid in serum. Microchimica Acta 164: 1-6
    • (2009) Microchimica Acta , vol.164 , pp. 1-6
    • Zhao, Y.1    Yang, X.2    Lu, W.3


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