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Volumn 58, Issue 1, 2004, Pages 110-116

Effects of water-soluble fractions of diesel oil on the antioxidant defenses of the goldfish, Carassius auratus

Author keywords

Antioxidant defense system; Exposure; Fish; Oil

Indexed keywords

BIOLOGICAL MARKER; DIESEL FUEL; GLUTATHIONE; GLUTATHIONE TRANSFERASE; WATER;

EID: 1842840037     PISSN: 01476513     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ecoenv.2003.08.025     Document Type: Article
Times cited : (102)

References (38)
  • 1
    • 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
  • 2
    • 0033013340 scopus 로고    scopus 로고
    • Crude oil exposure affects air-breathing frequency, blood phosphate levels and ion regulation in an air-breathing teleost fish, Hoplosternum littorale
    • Brauner C.J., Ballantyne C.L., Vijayan M.M., Val A.L. Crude oil exposure affects air-breathing frequency, blood phosphate levels and ion regulation in an air-breathing teleost fish, Hoplosternum littorale. Comp. Biochem. Physiol. 123:1999;127-134.
    • (1999) Comp. Biochem. Physiol. , vol.123 , pp. 127-134
    • Brauner, C.J.1    Ballantyne, C.L.2    Vijayan, M.M.3    Val, A.L.4
  • 3
    • 0022272480 scopus 로고
    • Glutathione reductase
    • Meister A. New York: Academic Press
    • Carlberg I., Mannervik B. Glutathione reductase. Meister A. Methods in Enzymology. Vol. 113:1985;484-490 Academic Press, New York.
    • (1985) Methods in Enzymology , vol.113 , pp. 484-490
    • Carlberg, I.1    Mannervik, B.2
  • 4
    • 45249127349 scopus 로고
    • Biochemical responses in aquatic animals: A review of determinants of oxidative stress
    • Di Giulio R.T., Washburn P.C., Wenning R.J. Biochemical responses in aquatic animals. a review of determinants of oxidative stress Environ. Toxicol. Chem. 8:1989;1103-1123.
    • (1989) Environ. Toxicol. Chem. , vol.8 , pp. 1103-1123
    • Di Giulio, R.T.1    Washburn, P.C.2    Wenning, R.J.3
  • 5
    • 0030824222 scopus 로고    scopus 로고
    • Antioxidant enzymes, glutathione and lipid peroxidation as relevant biomarkers of experimental or field exposure in the gills and the digestive gland of the freshwater bivalve unio tumidus
    • Doyotte A., Cossu C., Jacquin M.C., Babut M., Vasseur P. Antioxidant enzymes, glutathione and lipid peroxidation as relevant biomarkers of experimental or field exposure in the gills and the digestive gland of the freshwater bivalve unio tumidus. Aquat. Toxicol. 39:1997;93-110.
    • (1997) Aquat. Toxicol. , vol.39 , pp. 93-110
    • Doyotte, A.1    Cossu, C.2    Jacquin, M.C.3    Babut, M.4    Vasseur, P.5
  • 6
    • 0020858347 scopus 로고
    • Petroleum effects on marine mammals
    • Engelhardt F.R. Petroleum effects on marine mammals. Aquat. Toxicol. 4:1983;199-217.
    • (1983) Aquat. Toxicol. , vol.4 , pp. 199-217
    • Engelhardt, F.R.1
  • 7
    • 0034210998 scopus 로고    scopus 로고
    • Toxicity of third-generation dispersants and dispersed Egyptian crude oil on Red Sea coral larvae
    • Epstein N., Bak R.P.M., Rinkevich B. Toxicity of third-generation dispersants and dispersed Egyptian crude oil on Red Sea coral larvae. Mar. Pollut. Bull. 40:2000;497-503.
    • (2000) Mar. Pollut. Bull. , vol.40 , pp. 497-503
    • Epstein, N.1    Bak, R.P.M.2    Rinkevich, B.3
  • 9
    • 0026575011 scopus 로고
    • Insect glutathione S-transferases: Biochemical characteristics of the major forms of houseflies susceptible and resistant to insecticides
    • Fournier D., Bride J.M., Poirie M., Berge J.B., Plapp F.W. Insect glutathione S-transferases. biochemical characteristics of the major forms of houseflies susceptible and resistant to insecticides J. Biol. Chem. 267:1992;1840-1845.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1840-1845
    • Fournier, D.1    Bride, J.M.2    Poirie, M.3    Berge, J.B.4    Plapp, F.W.5
  • 10
    • 0008931425 scopus 로고    scopus 로고
    • Species characteristics of hepatic biotransformation enzymes in two tropical freshwater teleosts, tilapia (Oreochromis niloticus) and mudfish (Clarias anguillaris)
    • Gadagbui B.K.M., Addy M., GoksΦyr A. Species characteristics of hepatic biotransformation enzymes in two tropical freshwater teleosts, tilapia (Oreochromis niloticus) and mudfish (Clarias anguillaris). Comp. Biochem. Physiol. 114c:1996;201-211.
    • (1996) Comp. Biochem. Physiol. , vol.114 , pp. 201-211
    • Gadagbui, B.K.M.1    Addy, M.2    Goksoyr, A.3
  • 11
    • 0028935020 scopus 로고
    • Glutathione peroxidase and other antioxidant enzyme function in marine invertebrates (Mytilus edulis, Pecten maximus, carcinus maenas and Asterias rubens)
    • Gamble S.C., Goldfarb P.S., Porte C., Livingstone D.R. Glutathione peroxidase and other antioxidant enzyme function in marine invertebrates (Mytilus edulis, Pecten maximus, carcinus maenas and Asterias rubens). Mar. Environ. Res. 39:1995;191-195.
    • (1995) Mar. Environ. Res. , vol.39 , pp. 191-195
    • Gamble, S.C.1    Goldfarb, P.S.2    Porte, C.3    Livingstone, D.R.4
  • 13
    • 0016275313 scopus 로고
    • Glutathione S-transferases: The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., 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
  • 14
    • 0016170551 scopus 로고
    • Effect of dietary selenium and erythrocyte and liver glutathione peroxidase in the rat
    • Hafeman D.G., Sunde R.A., Hoekstra W.G. Effect of dietary selenium and erythrocyte and liver glutathione peroxidase in the rat. J. Nutr. 104:1973;580.
    • (1973) J. Nutr. , vol.104 , pp. 580
    • Hafeman, D.G.1    Sunde, R.A.2    Hoekstra, W.G.3
  • 15
    • 0029445091 scopus 로고
    • Effects of an organophosphate on the antioxidant system in fish tissues
    • Hai D.Q., Varga I.S., Matkovics B. Effects of an organophosphate on the antioxidant system in fish tissues. Acta Biol. Hung. 46:1995;39-50.
    • (1995) Acta Biol. Hung. , vol.46 , pp. 39-50
    • Hai, D.Q.1    Varga, I.S.2    Matkovics, B.3
  • 16
    • 0032787401 scopus 로고    scopus 로고
    • Evaluation of detoxification enzyme levels in Egyptian catfish, Clarias lazera, exposed to dimethoate
    • Hamed R.R., Elawa S.E., Farid N.M. Evaluation of detoxification enzyme levels in Egyptian catfish, Clarias lazera, exposed to dimethoate. Bull. Environ. Contam. Toxicol. 63:1999;789-796.
    • (1999) Bull. Environ. Contam. Toxicol. , vol.63 , pp. 789-796
    • Hamed, R.R.1    Elawa, S.E.2    Farid, N.M.3
  • 17
    • 0028291743 scopus 로고
    • Glutathione-dependent defense in channel catfish (Ictalurus punctatus) and brown bullhead (Ameriurius nebulosus)
    • Hasspieler B.M., Behar J.V., Di Giulio R.T. Glutathione-dependent defense in channel catfish (Ictalurus punctatus) and brown bullhead (Ameriurius nebulosus). Ecotoxicol. Environ. Saf. 28:1994;82-90.
    • (1994) Ecotoxicol. Environ. Saf. , vol.28 , pp. 82-90
    • Hasspieler, B.M.1    Behar, J.V.2    Di Giulio, R.T.3
  • 18
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., Hilf R. 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.2
  • 20
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptive response to hydrogen peroxide: Analysis of acatalasaemic saccharomyces cerevisiae
    • Izawa S., Inoue Y., Kimura A. Importance of catalase in the adaptive response to hydrogen peroxide. analysis of acatalasaemic saccharomyces cerevisiae Biochem. J. 320:1996;61-67.
    • (1996) Biochem. J. , vol.320 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 22
    • 0001557130 scopus 로고
    • Lipid peroxidation: Mechanisms, analysis, enzymology and biological relevance
    • H. Sies. London: Academic Press
    • Kappus H. Lipid peroxidation. mechanisms, analysis, enzymology and biological relevance Sies H. Oxidative Stress. 1985;273-310 Academic Press, London.
    • (1985) Oxidative Stress , pp. 273-310
    • Kappus, H.1
  • 23
    • 0030752006 scopus 로고    scopus 로고
    • Transport of glutathione conjugates and glucuronides by the multidrug resistance proteins MRP1 and MRP2
    • Keppler D., Leier I., Jedlitschky G. Transport of glutathione conjugates and glucuronides by the multidrug resistance proteins MRP1 and MRP2. Biol. Chem. 378:1997;787-791.
    • (1997) Biol. Chem. , vol.378 , pp. 787-791
    • Keppler, D.1    Leier, I.2    Jedlitschky, G.3
  • 24
    • 0025925851 scopus 로고
    • Long term effects of crude oil on common murres (Uria aalge) following rehabilitation
    • Khan R.A., Ryan P. Long term effects of crude oil on common murres (Uria aalge) following rehabilitation. Bull. Environ. Contam. Toxicol. 46:1991;216-222.
    • (1991) Bull. Environ. Contam. Toxicol. , vol.46 , pp. 216-222
    • Khan, R.A.1    Ryan, P.2
  • 25
    • 0023241638 scopus 로고
    • The hepatotoxic potential of a Prudhoe Bay crude oil: Effect on mouse liver weight and composition
    • Khan S., Irfan M., Rahimtula A.D. The hepatotoxic potential of a Prudhoe Bay crude oil. effect on mouse liver weight and composition Toxicology. 46:1987;95-105.
    • (1987) Toxicology , vol.46 , pp. 95-105
    • Khan, S.1    Irfan, M.2    Rahimtula, A.D.3
  • 26
    • 0029841209 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione metabolism and its role in hepatotoxicity
    • Kretzschmar M. Regulation of hepatic glutathione metabolism and its role in hepatotoxicity. Exp. Toxicol. Pathol. 48:1996;439-446.
    • (1996) Exp. Toxicol. Pathol. , vol.48 , pp. 439-446
    • Kretzschmar, M.1
  • 28
    • 0027333610 scopus 로고
    • Pro-oxidant, antioxidant and 7-ethoxyresorufin O-deethylase (EROD) activity responses in liver of dab (Limanda limanda) exposed to sediment contaminated with hydrocarbons and other chemicals
    • Livingstone D.R., Lemaire P., Matthews A.A., Peters L., Bucke D., Law R.J. Pro-oxidant, antioxidant and 7-ethoxyresorufin O-deethylase (EROD) activity responses in liver of dab (Limanda limanda) exposed to sediment contaminated with hydrocarbons and other chemicals. Mar. Pollut. Bull. 26:1993;602-606.
    • (1993) Mar. Pollut. Bull. , vol.26 , pp. 602-606
    • Livingstone, D.R.1    Lemaire, P.2    Matthews, A.A.3    Peters, L.4    Bucke, D.5    Law, R.J.6
  • 29
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S., Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47:1974;469-474.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 30
    • 0002938483 scopus 로고
    • Mammals as bioindicators of environmental toxicity
    • H.H. Genoways. New York: Plenum
    • McBee K., Bickham J.W. Mammals as bioindicators of environmental toxicity. Genoways H.H. Current Mammalogy. 1990;37-88 Plenum, New York.
    • (1990) Current Mammalogy , pp. 37-88
    • McBee, K.1    Bickham, J.W.2
  • 31
    • 0025896938 scopus 로고
    • Responses of mixed-function oxygenase and antioxidase enzyme system of Mytilus sp. to organic pollution
    • Porte C., Sole M., Albaiges J., Livingstone D.R. Responses of mixed-function oxygenase and antioxidase enzyme system of Mytilus sp. to organic pollution. Comp. Biochem. Physiol. C. 100:1991;183-186.
    • (1991) Comp. Biochem. Physiol. C , vol.100 , pp. 183-186
    • Porte, C.1    Sole, M.2    Albaiges, J.3    Livingstone, D.R.4
  • 32
    • 0031942274 scopus 로고    scopus 로고
    • Lysosomal and antioxidant responses to metals in the Antarctic Scallop Adamussium colbecki
    • Regoli F., Nigro M., Orlando E. Lysosomal and antioxidant responses to metals in the Antarctic Scallop Adamussium colbecki. Aquat. Toxicol. 40:1998;375-392.
    • (1998) Aquat. Toxicol. , vol.40 , pp. 375-392
    • Regoli, F.1    Nigro, M.2    Orlando, E.3
  • 34
    • 0000340531 scopus 로고
    • Molecular responses to environmental contamination: Enzyme and protein synthesis as indicators of chemical exposure and effects
    • R.A. Huggett, P.M. Kimerle, P.M. Jr. Mehrle, & H.L. Bergman. Boca Raton, FL: Lewis
    • Stegeman J.J., Marius Broumer Di., Giulio R.T. Molecular responses to environmental contamination. enzyme and protein synthesis as indicators of chemical exposure and effects Huggett R.A., Kimerle P.M., Mehrle P.M. Jr., Bergman H.L. Biomarkers, Biochemical, Physiological and Histological Markers of Anthropogenic Stress. 1992;235-335 Lewis, Boca Raton, FL.
    • (1992) Biomarkers, Biochemical, Physiological and Histological Markers of Anthropogenic Stress , pp. 235-335
    • Stegeman, J.J.1    Marius Broumer, Di.2    Giulio, R.T.3
  • 35
    • 0028788250 scopus 로고
    • Acute and subchronic toxicity of naturally weathered Exxon Valdez crude oil in mallards and ferrets
    • Stubblefield W.A., Hancock G.A., Ford W.H., Ringer R.K. Acute and subchronic toxicity of naturally weathered Exxon Valdez crude oil in mallards and ferrets. Environ. Toxicol. Chem. 14:1995;1941-1950.
    • (1995) Environ. Toxicol. Chem. , vol.14 , pp. 1941-1950
    • Stubblefield, W.A.1    Hancock, G.A.2    Ford, W.H.3    Ringer, R.K.4
  • 37
    • 0000514958 scopus 로고
    • Prooxidant and antioxidant mechanism in aquatic organism
    • Winston G.W., Di Giulio R.T. Prooxidant and antioxidant mechanism in aquatic organism. Aquat. Toxicol. 24:1991;143-152.
    • (1991) Aquat. Toxicol. , vol.24 , pp. 143-152
    • Winston, G.W.1    Di Giulio, R.T.2
  • 38
    • 0002157330 scopus 로고    scopus 로고
    • Determination of catalase activity and catalase inhibition by ultraviolet spectrophotometry
    • Xu J.B., Yuan X.F., Lang P.Z. Determination of catalase activity and catalase inhibition by ultraviolet spectrophotometry. Chin. Environ. Chem. 16:1997;73-76.
    • (1997) Chin. Environ. Chem. , vol.16 , pp. 73-76
    • Xu, J.B.1    Yuan, X.F.2    Lang, P.Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.