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Volumn 174, Issue 2, 2008, Pages 88-97

Amelioration of cadmium-induced cardiac impairment by taurine

Author keywords

Antioxidant; Cadmium; Cardiac dysfunction; Cardiac protection; Taurine

Indexed keywords

ASCORBIC ACID; CADMIUM CHLORIDE; CARBONYL DERIVATIVE; CATALASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; IRON; SUPEROXIDE DISMUTASE; TAURINE; TRIACYLGLYCEROL;

EID: 46149086734     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.05.005     Document Type: Article
Times cited : (67)

References (60)
  • 1
    • 0026297317 scopus 로고
    • Environmental pollutants and diseases. A cell biological approach using chronic cadmium exposure in the animal model as a paradigm case
    • Morselt A.F. Environmental pollutants and diseases. A cell biological approach using chronic cadmium exposure in the animal model as a paradigm case. Toxicology 70 (1991) 1-132
    • (1991) Toxicology , vol.70 , pp. 1-132
    • Morselt, A.F.1
  • 3
    • 0003494944 scopus 로고
    • WHO Regional Office for Europe, Copenhagen
    • WHO. Air Quality Guidelines (1987), WHO Regional Office for Europe, Copenhagen
    • (1987) Air Quality Guidelines
    • WHO1
  • 4
    • 0038349938 scopus 로고    scopus 로고
    • Toxic metals and antioxidants. Part II. The role of antioxidants in arsenic and cadmium toxicity
    • Patrick L. Toxic metals and antioxidants. Part II. The role of antioxidants in arsenic and cadmium toxicity. Altern. Med. Rev. 8 (2003) 106-128
    • (2003) Altern. Med. Rev. , vol.8 , pp. 106-128
    • Patrick, L.1
  • 5
    • 0035166619 scopus 로고    scopus 로고
    • Risk factors and incident coronary heart disease in Chinese, Malay and Asian Indian males: the Singapore Cardiovascular Cohort Study
    • Lee J., Heng D., Chia K.S., Chew S.K., Tan B.Y., and Hughes K. Risk factors and incident coronary heart disease in Chinese, Malay and Asian Indian males: the Singapore Cardiovascular Cohort Study. Int. J. Epidemiol. 30 (2001) 983-988
    • (2001) Int. J. Epidemiol. , vol.30 , pp. 983-988
    • Lee, J.1    Heng, D.2    Chia, K.S.3    Chew, S.K.4    Tan, B.Y.5    Hughes, K.6
  • 6
    • 33749347262 scopus 로고    scopus 로고
    • Environmental cardiology: studying mechanistic links between pollution and heart disease
    • Bhatnagar A. Environmental cardiology: studying mechanistic links between pollution and heart disease. Cir. Res. 99 (2006) 692-705
    • (2006) Cir. Res. , vol.99 , pp. 692-705
    • Bhatnagar, A.1
  • 7
    • 0026859475 scopus 로고
    • The role of cadmium in induction of atherosclerosis in rabbits
    • Subramanyam G., Bhaskar M., and Govindappa S. The role of cadmium in induction of atherosclerosis in rabbits. Ind. Heart J. 44 (1992) 177-180
    • (1992) Ind. Heart J. , vol.44 , pp. 177-180
    • Subramanyam, G.1    Bhaskar, M.2    Govindappa, S.3
  • 8
    • 0025056419 scopus 로고
    • Effect of occupational exposure to lead, zinc and cadmium on various indicators of the circulatory system of metallurgical workers
    • Sroczynski J., Biskupek K., Piotrowski J., and Rudzki H. Effect of occupational exposure to lead, zinc and cadmium on various indicators of the circulatory system of metallurgical workers. Med. Pr. 41 (1990) 152-158
    • (1990) Med. Pr. , vol.41 , pp. 152-158
    • Sroczynski, J.1    Biskupek, K.2    Piotrowski, J.3    Rudzki, H.4
  • 9
    • 0023522370 scopus 로고
    • Heavy metal and trace element deviations. A comparison of idiopathic dilated cardiomyopathy and coronary heart diseases
    • Smetana R., Glogar D., Weidinger F., and Meisinger V. Heavy metal and trace element deviations. A comparison of idiopathic dilated cardiomyopathy and coronary heart diseases. Wien. Med. Wochenschr. 137 (1987) 553-557
    • (1987) Wien. Med. Wochenschr. , vol.137 , pp. 553-557
    • Smetana, R.1    Glogar, D.2    Weidinger, F.3    Meisinger, V.4
  • 11
    • 0026595620 scopus 로고
    • Physiological action of taurine
    • Huxtable R.J. Physiological action of taurine. Physiol. Rev. 72 (1992) 101-163
    • (1992) Physiol. Rev. , vol.72 , pp. 101-163
    • Huxtable, R.J.1
  • 12
    • 0020544865 scopus 로고
    • Effects of taurine and taurine antagonists on some respiratory and cardiovascular parameters
    • Wessberg P., Hedner T., Hedner J., and Jonason. Effects of taurine and taurine antagonists on some respiratory and cardiovascular parameters. Life Sci. 33 (1983) 1649-1656
    • (1983) Life Sci. , vol.33 , pp. 1649-1656
    • Wessberg, P.1    Hedner, T.2    Hedner, J.3    Jonason4
  • 13
    • 0028921717 scopus 로고
    • The in vivo and in vitro protective properties of taurine
    • Timbrell J.A., Seabra V., and Watereld C.J. The in vivo and in vitro protective properties of taurine. Gen. Pharmacol. 26 (1995) 453-462
    • (1995) Gen. Pharmacol. , vol.26 , pp. 453-462
    • Timbrell, J.A.1    Seabra, V.2    Watereld, C.J.3
  • 16
    • 0031970082 scopus 로고    scopus 로고
    • Protective effects of taurine against reperfusion-induced arrhythmias in isolated ischemic rat heart
    • Chahine R., and Feng J. Protective effects of taurine against reperfusion-induced arrhythmias in isolated ischemic rat heart. Arzneimittelforschung 48 (1998) 360-364
    • (1998) Arzneimittelforschung , vol.48 , pp. 360-364
    • Chahine, R.1    Feng, J.2
  • 17
    • 0032039928 scopus 로고    scopus 로고
    • Therapeutic applications of taurine
    • Birdsall T.C. Therapeutic applications of taurine. Altern. Med. Rev. 3 (1998) 128-136
    • (1998) Altern. Med. Rev. , vol.3 , pp. 128-136
    • Birdsall, T.C.1
  • 19
    • 0034585558 scopus 로고    scopus 로고
    • Taurine reduces atherosclerotic lesion development in apolipoprotein E-deficient mice
    • Kondo Y., Murakami S., Oda H., and Nagate T. Taurine reduces atherosclerotic lesion development in apolipoprotein E-deficient mice. Adv. Exp. Med. Biol. 483 (2000) 123-126
    • (2000) Adv. Exp. Med. Biol. , vol.483 , pp. 123-126
    • Kondo, Y.1    Murakami, S.2    Oda, H.3    Nagate, T.4
  • 20
    • 0019946061 scopus 로고
    • Diet and biosynthesis as sources of taurine in the mouse
    • Huxtable R.J., and Lippincott S.E. Diet and biosynthesis as sources of taurine in the mouse. J. Nutr. 112 (1982) 1003-1010
    • (1982) J. Nutr. , vol.112 , pp. 1003-1010
    • Huxtable, R.J.1    Lippincott, S.E.2
  • 21
    • 33846070110 scopus 로고    scopus 로고
    • Cytoprotective and antioxidant role of diallyl tetrasulfide on cadmium induced renal injury: an in vivo and in vitro study
    • Pari L., Murugavel P., Sitasawad S.L., and Kumar K.S. Cytoprotective and antioxidant role of diallyl tetrasulfide on cadmium induced renal injury: an in vivo and in vitro study. Life Sci. 80 (2007) 650-658
    • (2007) Life Sci. , vol.80 , pp. 650-658
    • Pari, L.1    Murugavel, P.2    Sitasawad, S.L.3    Kumar, K.S.4
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0031729201 scopus 로고    scopus 로고
    • Ferric reducing/antioxidant power assay: direct measure of total antioxidant activity of biological fluids and modified version for simultaneous measurement of total antioxidant power and ascorbic acid concentration
    • Benzie I.F.F., and Strain J.J. Ferric reducing/antioxidant power assay: direct measure of total antioxidant activity of biological fluids and modified version for simultaneous measurement of total antioxidant power and ascorbic acid concentration. Methods Enzymol. 299 (1999) 15-27
    • (1999) Methods Enzymol. , vol.299 , pp. 15-27
    • Benzie, I.F.F.1    Strain, J.J.2
  • 24
    • 0025127633 scopus 로고
    • Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal
    • Esterbauer H., and Cheeseman K.H. Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal. Methods Enzymol. 186 (1990) 407-421
    • (1990) Methods Enzymol. , vol.186 , pp. 407-421
    • Esterbauer, H.1    Cheeseman, K.H.2
  • 25
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehydes-3-phosphate dehydrogenase
    • Uchida K., and Stadtman E.R. Covalent attachment of 4-hydroxynonenal to glyceraldehydes-3-phosphate dehydrogenase. J. Biol. Chem. 268 (1993) 6388-6393
    • (1993) J. Biol. Chem. , vol.268 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 26
    • 0015530358 scopus 로고
    • The occurrence of superoxide anion in the reaction of reduced phenazine methosulfate and molecular oxygen
    • Nishikimi M., Rao N.A., and Yagi K. The occurrence of superoxide anion in the reaction of reduced phenazine methosulfate and molecular oxygen. Biochem. Biophys. Res. Commun. 46 (1972) 849-854
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 849-854
    • Nishikimi, M.1    Rao, N.A.2    Yagi, K.3
  • 27
    • 0021681627 scopus 로고
    • A modified spectrophotometric assay of superoxide dismutase
    • Kakkar P., Das B., and Viswanathan P.N. A modified spectrophotometric assay of superoxide dismutase. Ind. J. Biochem. Biophys. 21 (1984) 130-132
    • (1984) Ind. J. Biochem. Biophys. , vol.21 , pp. 130-132
    • Kakkar, P.1    Das, B.2    Viswanathan, P.N.3
  • 28
    • 0015352861 scopus 로고
    • Human erythrocyte catalase: an improved method of isolation and a revaluation of reported properties
    • Bonaventura J., Schroeder W.A., and Fang S. Human erythrocyte catalase: an improved method of isolation and a revaluation of reported properties. Arch. Biochem. Biophys. 150 (1972) 606-617
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 606-617
    • Bonaventura, J.1    Schroeder, W.A.2    Fang, S.3
  • 29
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 30
    • 0024199997 scopus 로고
    • Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis (2-nitrobenzoic acid)
    • Smith I.K., Vierheller T.L., and Thorne C.A. Assay of glutathione reductase in crude tissue homogenates using 5,5′-dithiobis (2-nitrobenzoic acid). Anal. Biochem. 175 (1988) 408-413
    • (1988) Anal. Biochem. , vol.175 , pp. 408-413
    • Smith, I.K.1    Vierheller, T.L.2    Thorne, C.A.3
  • 31
    • 0021288821 scopus 로고
    • Assay of glutathione peroxidase
    • Flohe L., and Gunzler W.A. Assay of glutathione peroxidase. Methods Enzymol. 105 (1984) 114-121
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 32
    • 0020435680 scopus 로고
    • Glucose-6-phosphate dehydrogenase from mouse
    • Lee C.Y. Glucose-6-phosphate dehydrogenase from mouse. Methods Enzymol. 89 (1982) 252-257
    • (1982) Methods Enzymol. , vol.89 , pp. 252-257
    • Lee, C.Y.1
  • 34
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., and Hilf R.A. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 74 (1976) 214-226
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.A.2
  • 35
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and non-protein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak J., and Lindsay R.H. Estimation of total, protein-bound, and non-protein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem. 24/25 (1958) 192-205
    • (1958) Anal. Biochem. , vol.24-25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 36
    • 0031550256 scopus 로고    scopus 로고
    • Reactive oxygen species participate in peroxinitrile induced apoptosis in HL 60 cells
    • Lin K.T., Xue J.Y., Sun F.F., and Wong P.Y.K. Reactive oxygen species participate in peroxinitrile induced apoptosis in HL 60 cells. Biochem. Biophys. Res. Commun. 230 (1997) 115-119
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 115-119
    • Lin, K.T.1    Xue, J.Y.2    Sun, F.F.3    Wong, P.Y.K.4
  • 37
    • 0023612470 scopus 로고
    • Gene induction by gamma-irradiation leads to DNA fragmentation in lymphocytes
    • Sellins K.S., and Cohen J.J. Gene induction by gamma-irradiation leads to DNA fragmentation in lymphocytes. J. Immunol. 139 (1987) 3199-3206
    • (1987) J. Immunol. , vol.139 , pp. 3199-3206
    • Sellins, K.S.1    Cohen, J.J.2
  • 38
    • 46149083297 scopus 로고    scopus 로고
    • http://www.healingdaily.com/detoxification-diet/taurine.htm
  • 39
    • 0037200774 scopus 로고    scopus 로고
    • Molecular inhibitory mechanisms of antioxidant enzymes in rat liver and kidney by cadmium
    • Casalino E., Calzaretti G., Sblano C., and Landriscina C. Molecular inhibitory mechanisms of antioxidant enzymes in rat liver and kidney by cadmium. Toxicology 179 (2002) 37-50
    • (2002) Toxicology , vol.179 , pp. 37-50
    • Casalino, E.1    Calzaretti, G.2    Sblano, C.3    Landriscina, C.4
  • 40
    • 0031572856 scopus 로고    scopus 로고
    • Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation
    • Casalino E., Sblano C., and Landriscina C. Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation. Arch. Biochem. Biophys. 346 (1997) 171-179
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 171-179
    • Casalino, E.1    Sblano, C.2    Landriscina, C.3
  • 41
    • 0242657585 scopus 로고    scopus 로고
    • Action of NO and TNF-alpha release of rats with cadmium loading in malfunction of multiple system organ
    • Chen L., Zhou J., Gao W., and Jiang Y.Z. Action of NO and TNF-alpha release of rats with cadmium loading in malfunction of multiple system organ. Sheng Li Xue Bao 25/55 (2003) 535-540
    • (2003) Sheng Li Xue Bao , vol.25-55 , pp. 535-540
    • Chen, L.1    Zhou, J.2    Gao, W.3    Jiang, Y.Z.4
  • 42
    • 0033670137 scopus 로고    scopus 로고
    • Inhibition of inducible nitric oxide synthase in the human intestinal epithelial cell line, DLD-1, by the inducers of heme oxygenase 1, bismuth salts, heme, and nitric oxide donors
    • Cavicchi M., Gibbs L., and Whittle B.J. Inhibition of inducible nitric oxide synthase in the human intestinal epithelial cell line, DLD-1, by the inducers of heme oxygenase 1, bismuth salts, heme, and nitric oxide donors. Gut 47 (2000) 771-778
    • (2000) Gut , vol.47 , pp. 771-778
    • Cavicchi, M.1    Gibbs, L.2    Whittle, B.J.3
  • 43
    • 0031962250 scopus 로고    scopus 로고
    • Induction of c-fos protooncogene in mesangial cells by cadmium
    • Wang Z., and Templeton D.M. Induction of c-fos protooncogene in mesangial cells by cadmium. J. Biol. Chem. 273 (1998) 73-79
    • (1998) J. Biol. Chem. , vol.273 , pp. 73-79
    • Wang, Z.1    Templeton, D.M.2
  • 44
    • 0025804981 scopus 로고
    • Study of the interaction of cadmium with membranebound succinate dehydrogenase
    • Jay D., Zamorano R., Munoz E., Gleason R., and Boldu J.L. Study of the interaction of cadmium with membranebound succinate dehydrogenase. J. Bioenerg. Biomembr. 23 (1991) 381-389
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 381-389
    • Jay, D.1    Zamorano, R.2    Munoz, E.3    Gleason, R.4    Boldu, J.L.5
  • 46
    • 0033833788 scopus 로고    scopus 로고
    • Oxidative stress and cardiac disease
    • Lefer D.J., and Granger D.N. Oxidative stress and cardiac disease. Am. J. Med. 109 (2000) 315-323
    • (2000) Am. J. Med. , vol.109 , pp. 315-323
    • Lefer, D.J.1    Granger, D.N.2
  • 47
    • 0037400919 scopus 로고    scopus 로고
    • Melatonin: a novel protective agent against oxidative injury of the ischemic/reperfused heart
    • Reiter R.J., and Tan D.X. Melatonin: a novel protective agent against oxidative injury of the ischemic/reperfused heart. Cardiovasc. Res. 58 (2003) 10-19
    • (2003) Cardiovasc. Res. , vol.58 , pp. 10-19
    • Reiter, R.J.1    Tan, D.X.2
  • 48
    • 0022921079 scopus 로고
    • Consequences of cadmium toxicity in rat hepatocytes: mitochondrial dysfunction and lipid peroxidation
    • Muller L. Consequences of cadmium toxicity in rat hepatocytes: mitochondrial dysfunction and lipid peroxidation. Toxicology 40 (1986) 285-295
    • (1986) Toxicology , vol.40 , pp. 285-295
    • Muller, L.1
  • 49
    • 0027392846 scopus 로고
    • Alterations in cytoskeletal protein sulfhydryls and cellular glutathione in cultured cells exposed to cadmium and nickel ions
    • Li W., Zhao Y., and Chou I.N. Alterations in cytoskeletal protein sulfhydryls and cellular glutathione in cultured cells exposed to cadmium and nickel ions. Toxicology 77 (1993) 65-79
    • (1993) Toxicology , vol.77 , pp. 65-79
    • Li, W.1    Zhao, Y.2    Chou, I.N.3
  • 50
    • 0023543145 scopus 로고
    • Possible role of regional superoxide dismutase activity and lipid peroxide levels in cadmium neurotoxicity: in vivo and in vitro studies in growing rats
    • Shukla G.S., Hussain T., and Chandra S.V. Possible role of regional superoxide dismutase activity and lipid peroxide levels in cadmium neurotoxicity: in vivo and in vitro studies in growing rats. Life Sci. 41 (1987) 2215-2221
    • (1987) Life Sci. , vol.41 , pp. 2215-2221
    • Shukla, G.S.1    Hussain, T.2    Chandra, S.V.3
  • 51
    • 0026747099 scopus 로고
    • Cadmium-induced DNA strand damage in cultured liver cells: reduction in cadmium genotoxicity following zinc pretreatment
    • Coogan T.P., Bare R.M., and Waalkes M.P. Cadmium-induced DNA strand damage in cultured liver cells: reduction in cadmium genotoxicity following zinc pretreatment. Toxicol. Appl. Pharmacol. 113 (1992) 227-233
    • (1992) Toxicol. Appl. Pharmacol. , vol.113 , pp. 227-233
    • Coogan, T.P.1    Bare, R.M.2    Waalkes, M.P.3
  • 52
    • 0025922756 scopus 로고
    • 113Cd-NMR investigation of a cadmium-substitution copper, zinc-containing superoxide dismutase from yeast
    • Confod P., Baurer R., Danielsen E., Larsen E., and Bierrum M.J. 113Cd-NMR investigation of a cadmium-substitution copper, zinc-containing superoxide dismutase from yeast. Eur. J. Biochem. 198 (1991) 607-611
    • (1991) Eur. J. Biochem. , vol.198 , pp. 607-611
    • Confod, P.1    Baurer, R.2    Danielsen, E.3    Larsen, E.4    Bierrum, M.J.5
  • 53
    • 10544251069 scopus 로고    scopus 로고
    • Taurine attenuates nitric oxide- and reactive oxygen intermediate-dependent hepatocyte injury
    • Redmond H.P., Wang J.H., and Bouchier-Hayes D. Taurine attenuates nitric oxide- and reactive oxygen intermediate-dependent hepatocyte injury. Arch. Surg. 131 (1996) 1287-1288
    • (1996) Arch. Surg. , vol.131 , pp. 1287-1288
    • Redmond, H.P.1    Wang, J.H.2    Bouchier-Hayes, D.3
  • 54
    • 0028803246 scopus 로고
    • Taurine and ellagic acid: two differently acting natural antioxidants
    • Cozzi R., Ricordy R., Bartolini F., et al. Taurine and ellagic acid: two differently acting natural antioxidants. Environ. Mol. Mutagen. 26 (1995) 248-254
    • (1995) Environ. Mol. Mutagen. , vol.26 , pp. 248-254
    • Cozzi, R.1    Ricordy, R.2    Bartolini, F.3
  • 55
    • 0023697974 scopus 로고
    • The antioxidant action of taurine, hypotaurine and their metabolic precursors
    • Aruoma O.I., Halliwell B., Hoey B.M., and Butler J. The antioxidant action of taurine, hypotaurine and their metabolic precursors. Biochem. J. 256 (1988) 251-255
    • (1988) Biochem. J. , vol.256 , pp. 251-255
    • Aruoma, O.I.1    Halliwell, B.2    Hoey, B.M.3    Butler, J.4
  • 56
    • 0026692870 scopus 로고
    • Taurine protection of lungs in hamster models of oxidant injury: a morphologic time study of paraquat and bleomycin treatment
    • Lombardini J.B., Schaffer S.W., and Azuma J. (Eds), Plenum Press, New York
    • Gordon R.E., and Heller R.F. Taurine protection of lungs in hamster models of oxidant injury: a morphologic time study of paraquat and bleomycin treatment. In: Lombardini J.B., Schaffer S.W., and Azuma J. (Eds). Taurine: Nutritional Value and Mechanisms of Action (1992), Plenum Press, New York 319-323
    • (1992) Taurine: Nutritional Value and Mechanisms of Action , pp. 319-323
    • Gordon, R.E.1    Heller, R.F.2
  • 59
    • 0023110837 scopus 로고
    • Biologically significant scavenging of the myeloperoxidase derived oxidant hypochlorous acid by ascorbic acid
    • Halliwell B., Wasil M., and Grootveld M. Biologically significant scavenging of the myeloperoxidase derived oxidant hypochlorous acid by ascorbic acid. FEBS Lett. 213 (1987) 15-17
    • (1987) FEBS Lett. , vol.213 , pp. 15-17
    • Halliwell, B.1    Wasil, M.2    Grootveld, M.3
  • 60
    • 0031710731 scopus 로고    scopus 로고
    • Role of ascorbic acid in cadmium induced thyroid dysfunction and lipid peroxidation
    • Gupta P., and Kar A. Role of ascorbic acid in cadmium induced thyroid dysfunction and lipid peroxidation. J. Appl. Toxicol. 18 (1998) 317-320
    • (1998) J. Appl. Toxicol. , vol.18 , pp. 317-320
    • Gupta, P.1    Kar, A.2


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