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Volumn 85, Issue 6, 2011, Pages 983-989

Cobalt-induced oxidative stress in brain, liver and kidney of goldfish Carassius auratus

Author keywords

Antioxidant enzymes; Carbonyl proteins; Cobalt ions; Goldfish; Lipid peroxides; Oxidative stress

Indexed keywords

ANTIOXIDANTS; COBALT; ENZYMES; FISH; OXIDATION; OXIDATIVE STRESS; PEPTIDES; PEROXIDES;

EID: 80455155121     PISSN: 00456535     EISSN: 18791298     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2011.06.078     Document Type: Article
Times cited : (54)

References (66)
  • 1
    • 35548937284 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant defenses in goldfish liver in response to short-term exposure to arsenite
    • Bagnyukova T.V., Luzhna L.I., Pogribny I., Lushchak V.I. Oxidative stress and antioxidant defenses in goldfish liver in response to short-term exposure to arsenite. Environ. Mol. Mutagen. 2007, 4:658-665.
    • (2007) Environ. Mol. Mutagen. , vol.4 , pp. 658-665
    • Bagnyukova, T.V.1    Luzhna, L.I.2    Pogribny, I.3    Lushchak, V.I.4
  • 2
    • 0032605655 scopus 로고    scopus 로고
    • Structural and functional studies of monomeric mutant of Cu-Zn superoxide dismutase without Arg 143
    • Banci L., Bertini I., Del Conte R., Viezzoli M.S. Structural and functional studies of monomeric mutant of Cu-Zn superoxide dismutase without Arg 143. Biospectroscopy 1999, 5:S33-S41.
    • (1999) Biospectroscopy , vol.5
    • Banci, L.1    Bertini, I.2    Del Conte, R.3    Viezzoli, M.S.4
  • 4
    • 58149307941 scopus 로고    scopus 로고
    • Cobalt induces oxidative stress in isolated liver mitochondria responsible for permeability transition and intrinsic apoptosis in hepatocytes primary cultures
    • Battaglia V. Cobalt induces oxidative stress in isolated liver mitochondria responsible for permeability transition and intrinsic apoptosis in hepatocytes primary cultures. Int. J. Biochem. Cell Biol. 2009, 41:586-594.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 586-594
    • Battaglia, V.1
  • 5
    • 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. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0027092553 scopus 로고
    • A simple computer program with statistical test for the analysis of enzyme kinetics
    • Brooks S.P.J. A simple computer program with statistical test for the analysis of enzyme kinetics. Biotechniques 1992, 13:906-911.
    • (1992) Biotechniques , vol.13 , pp. 906-911
    • Brooks, S.P.J.1
  • 7
    • 0034304391 scopus 로고    scopus 로고
    • NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders; the role of oxidant/antioxidant balance
    • Calabrese V., Bates T.E., Stella A.M.G. NO synthase and NO-dependent signal pathways in brain aging and neurodegenerative disorders; the role of oxidant/antioxidant balance. Neurochem. Res. 2000, 25:1315-1341.
    • (2000) Neurochem. Res. , vol.25 , pp. 1315-1341
    • Calabrese, V.1    Bates, T.E.2    Stella, A.M.G.3
  • 10
    • 0034753669 scopus 로고    scopus 로고
    • Heme oxygenase is the main protective enzyme in rat liver upon 6-day administration of cobalt chloride
    • Christova T., Duridanova D., Braykova A., Setchenska M., Bolton T. Heme oxygenase is the main protective enzyme in rat liver upon 6-day administration of cobalt chloride. Arch. Toxicol. 2001, 75:445-451.
    • (2001) Arch. Toxicol. , vol.75 , pp. 445-451
    • Christova, T.1    Duridanova, D.2    Braykova, A.3    Setchenska, M.4    Bolton, T.5
  • 11
    • 0036190993 scopus 로고    scopus 로고
    • Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon acute cobalt chloride loading: comparison with rat liver
    • Christova T.Y., Duridanova D.B., Setchenska M.S. Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon acute cobalt chloride loading: comparison with rat liver. Comp. Biochem. Physiol. Pt. C 2002, 131:177-184.
    • (2002) Comp. Biochem. Physiol. Pt. C , vol.131 , pp. 177-184
    • Christova, T.Y.1    Duridanova, D.B.2    Setchenska, M.S.3
  • 12
    • 0037416672 scopus 로고    scopus 로고
    • Effect of cisplatin and cobalt chloride on antioxidant enzymes in the livers of Lewis lung carcinoma-bearing mice: protective role of heme oxygenase
    • Christova T.Y., Gorneva G.A., Taxirov S.I., Duridanova D.B., Setchenska M.S. Effect of cisplatin and cobalt chloride on antioxidant enzymes in the livers of Lewis lung carcinoma-bearing mice: protective role of heme oxygenase. Toxicol. Lett. 2003, 138:235-242.
    • (2003) Toxicol. Lett. , vol.138 , pp. 235-242
    • Christova, T.Y.1    Gorneva, G.A.2    Taxirov, S.I.3    Duridanova, D.B.4    Setchenska, M.S.5
  • 13
    • 0006474671 scopus 로고    scopus 로고
    • Branchial cobalt uptake in the carp Cyprinus carpio: effect of calcium channels blockers and calcium injection
    • Comhaire S., Blust R., Van Ginnken L., Verbost P.M., Vanderborght O.L.J. Branchial cobalt uptake in the carp Cyprinus carpio: effect of calcium channels blockers and calcium injection. Fish Physiol. Biochem. 1998, 18:1-13.
    • (1998) Fish Physiol. Biochem. , vol.18 , pp. 1-13
    • Comhaire, S.1    Blust, R.2    Van Ginnken, L.3    Verbost, P.M.4    Vanderborght, O.L.J.5
  • 14
    • 0001046328 scopus 로고
    • Individual and interactive lethal toxicity of cadmium, potassium permanganate and cobalt chloride to fish, worm and plankton
    • Das B.K., Kaviraj A. Individual and interactive lethal toxicity of cadmium, potassium permanganate and cobalt chloride to fish, worm and plankton. Geobios 1994, 21:223-227.
    • (1994) Geobios , vol.21 , pp. 223-227
    • Das, B.K.1    Kaviraj, A.2
  • 16
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 1997, 324:1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 18
    • 33644994476 scopus 로고    scopus 로고
    • Effect of cobalt and chromium ions on human MG-63 osteoblasts in vitro: morphology, cytotoxicity, and oxidative stress
    • Fleury C., Petit A., Mwale F., Antoniou J., Zukor D.J., Tabrizian M., Huk O.L. Effect of cobalt and chromium ions on human MG-63 osteoblasts in vitro: morphology, cytotoxicity, and oxidative stress. Biomaterials 2006, 27:3351-3360.
    • (2006) Biomaterials , vol.27 , pp. 3351-3360
    • Fleury, C.1    Petit, A.2    Mwale, F.3    Antoniou, J.4    Zukor, D.J.5    Tabrizian, M.6    Huk, O.L.7
  • 21
    • 0034961133 scopus 로고    scopus 로고
    • Production of superoxide anion, lipid peroxidation and DNA damage in the hepatic and brain tissues of rats after subchronic exposure to mixture of TCDD and its congeners
    • Hassoun E.A., Li F., Abushaban A., Stohs S.J. Production of superoxide anion, lipid peroxidation and DNA damage in the hepatic and brain tissues of rats after subchronic exposure to mixture of TCDD and its congeners. J. Appl. Toxicol. 2001, 21:211-219.
    • (2001) J. Appl. Toxicol. , vol.21 , pp. 211-219
    • Hassoun, E.A.1    Li, F.2    Abushaban, A.3    Stohs, S.J.4
  • 22
    • 0029114548 scopus 로고
    • Quantification of lipid peroxidation in tissue extracts based on Fe(III) xylenol orange complex formation
    • Hermes-Lima M., Willmore W.G., Storey K.B. Quantification of lipid peroxidation in tissue extracts based on Fe(III) xylenol orange complex formation. Free Radical Biol. Med. 1995, 19:271-280.
    • (1995) Free Radical Biol. Med. , vol.19 , pp. 271-280
    • Hermes-Lima, M.1    Willmore, W.G.2    Storey, K.B.3
  • 23
    • 0034751813 scopus 로고    scopus 로고
    • Mechanism, origin, and evolution of anoxia tolerance in animals
    • Hochachka P.W., Lutz P.L. Mechanism, origin, and evolution of anoxia tolerance in animals. Comp. Biochem. Physiol. Pt. B 2001, 130:435-459.
    • (2001) Comp. Biochem. Physiol. Pt. B , vol.130 , pp. 435-459
    • Hochachka, P.W.1    Lutz, P.L.2
  • 24
    • 0035793128 scopus 로고    scopus 로고
    • Interactions of metals and thiols in cell damage and glutathione distribution: potential of mercury toxicity by dithiothreitol
    • Hultberg B., Andersson A., Isaksson A. Interactions of metals and thiols in cell damage and glutathione distribution: potential of mercury toxicity by dithiothreitol. Toxicology 2001, 56:93-100.
    • (2001) Toxicology , vol.56 , pp. 93-100
    • Hultberg, B.1    Andersson, A.2    Isaksson, A.3
  • 26
    • 0035253381 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein
    • Ivan M., Kaelin W.G. The von Hippel-Lindau tumor suppressor protein. Curr. Opin. Genet. Dev. 2001, 11:27-34.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 27-34
    • Ivan, M.1    Kaelin, W.G.2
  • 29
    • 0029266693 scopus 로고
    • Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide
    • Lardinois O.M. Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide. Free Radical Res. 1995, 22:251-274.
    • (1995) Free Radical Res. , vol.22 , pp. 251-274
    • Lardinois, O.M.1
  • 32
    • 0024590274 scopus 로고
    • Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride
    • Lenz A.-G., Costabel U., Shaltiel S., Levine R.L. Determination of carbonyl groups in oxidatively modified proteins by reduction with tritiated sodium borohydride. Anal. Biochem. 1989, 177:419-425.
    • (1989) Anal. Biochem. , vol.177 , pp. 419-425
    • Lenz, A.-G.1    Costabel, U.2    Shaltiel, S.3    Levine, R.L.4
  • 33
    • 78049306575 scopus 로고    scopus 로고
    • Effect of a human pharmaceutical carbamazepine on antioxidant responses in brain of a model teleost in vitro: an efficient approach to biomonitoring
    • Li Z.H., Li P., Randak T. Effect of a human pharmaceutical carbamazepine on antioxidant responses in brain of a model teleost in vitro: an efficient approach to biomonitoring. J. Appl. Toxicol. 2010, 30:644-648.
    • (2010) J. Appl. Toxicol. , vol.30 , pp. 644-648
    • Li, Z.H.1    Li, P.2    Randak, T.3
  • 34
    • 77956187360 scopus 로고    scopus 로고
    • Biochemical and physiological responses in liver and muscle of rainbow trout after long-term exposure to propiconazole
    • Li Z.H., Zlabek V., Li P., Grabic R., Velisek J., Machova J., Randak T. Biochemical and physiological responses in liver and muscle of rainbow trout after long-term exposure to propiconazole. Ecotoxicol. Environ. Saf. 2010, 73:1391-1396.
    • (2010) Ecotoxicol. Environ. Saf. , vol.73 , pp. 1391-1396
    • Li, Z.H.1    Zlabek, V.2    Li, P.3    Grabic, R.4    Velisek, J.5    Machova, J.6    Randak, T.7
  • 35
    • 77955053269 scopus 로고    scopus 로고
    • Modulation of glutathione-related antioxidant defense system of fish chronically treated by the fungicide propiconazole
    • Li Z.H., Zlabek V., Grabic R., Li P., Randak T. Modulation of glutathione-related antioxidant defense system of fish chronically treated by the fungicide propiconazole. Comp. Biochem. Physiol. Pt. C 2010, 152:392-398.
    • (2010) Comp. Biochem. Physiol. Pt. C , vol.152 , pp. 392-398
    • Li, Z.H.1    Zlabek, V.2    Grabic, R.3    Li, P.4    Randak, T.5
  • 36
    • 77955056990 scopus 로고    scopus 로고
    • Ecotoxicological effects of short-term exposure to a human pharmaceutical Verapamil in juvenile rainbow trout (Oncorhynchus mykiss)
    • Li Z.H., Li P., Randak T. Ecotoxicological effects of short-term exposure to a human pharmaceutical Verapamil in juvenile rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. Pt. C 2010, 152:385-391.
    • (2010) Comp. Biochem. Physiol. Pt. C , vol.152 , pp. 385-391
    • Li, Z.H.1    Li, P.2    Randak, T.3
  • 37
    • 78649938431 scopus 로고    scopus 로고
    • Chronic toxicity of verapamil on juvenile rainbow trout (Oncorhynchus mykiss): effects on morphological indices, hematological parameters and antioxidant responses
    • Li Z.H., Velisek J., Zlabek V., Grabic R., Machova J., Kolarova J., Li P., Randak T. Chronic toxicity of verapamil on juvenile rainbow trout (Oncorhynchus mykiss): effects on morphological indices, hematological parameters and antioxidant responses. J. Hazard. Mater. 2011, 185:870-880.
    • (2011) J. Hazard. Mater. , vol.185 , pp. 870-880
    • Li, Z.H.1    Velisek, J.2    Zlabek, V.3    Grabic, R.4    Machova, J.5    Kolarova, J.6    Li, P.7    Randak, T.8
  • 40
    • 61549135236 scopus 로고    scopus 로고
    • Oxidative stress as a component of transition metal toxicity in fish
    • Nova Science Publishers Inc., Hauppaug, NY, USA, E.P. Svensson (Ed.)
    • Lushchak V.I. Oxidative stress as a component of transition metal toxicity in fish. Aquatic Toxicology Research Focus 2008, 1-29. Nova Science Publishers Inc., Hauppaug, NY, USA. E.P. Svensson (Ed.).
    • (2008) Aquatic Toxicology Research Focus , pp. 1-29
    • Lushchak, V.I.1
  • 41
    • 78650598564 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress: bacteria, fungi, plants and animals
    • Lushchak V.I. Adaptive response to oxidative stress: bacteria, fungi, plants and animals. Comp. Biochem. Physiol. Pt. C 2011, 153:175-190.
    • (2011) Comp. Biochem. Physiol. Pt. C , vol.153 , pp. 175-190
    • Lushchak, V.I.1
  • 42
    • 78649906789 scopus 로고    scopus 로고
    • Environmentally induced oxidative stress in aquatic animals
    • Lushchak V.I. Environmentally induced oxidative stress in aquatic animals. Aquat. Toxicol. 2011, 101(1):13-30.
    • (2011) Aquat. Toxicol. , vol.101 , Issue.1 , pp. 13-30
    • Lushchak, V.I.1
  • 43
    • 33645384675 scopus 로고    scopus 로고
    • Temperature increase results in oxidative stress in goldfish tissues: 1. Indices of oxidative stress
    • Lushchak V.I., Bagnyukova T.V. Temperature increase results in oxidative stress in goldfish tissues: 1. Indices of oxidative stress. Comp. Biochem. Physiol. Pt. C 2006, 143:30-35.
    • (2006) Comp. Biochem. Physiol. Pt. C , vol.143 , pp. 30-35
    • Lushchak, V.I.1    Bagnyukova, T.V.2
  • 44
    • 33745276255 scopus 로고    scopus 로고
    • Effects of different environmental oxygen levels on free radical processes in fish
    • Lushchak V.I., Bagnyukova T.V. Effects of different environmental oxygen levels on free radical processes in fish. Comp. Biochem. Physiol. Pt. B 2006, 144:283-289.
    • (2006) Comp. Biochem. Physiol. Pt. B , vol.144 , pp. 283-289
    • Lushchak, V.I.1    Bagnyukova, T.V.2
  • 45
    • 35649024751 scopus 로고    scopus 로고
    • Hypoxia induces oxidative stress in tissues of a goby fish, the rotan Percottus glenii
    • Lushchak V.I., Bagnyukova T.V. Hypoxia induces oxidative stress in tissues of a goby fish, the rotan Percottus glenii. Comp. Biochem. Physiol. Pt. B 2007, 148:390-397.
    • (2007) Comp. Biochem. Physiol. Pt. B , vol.148 , pp. 390-397
    • Lushchak, V.I.1    Bagnyukova, T.V.2
  • 46
    • 0034997803 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant defenses in goldfish Carassius auratus during anoxia and reoxygenation
    • Lushchak V.I., Lushchak L.P., Mota A.A., Hermes-Lima M. Oxidative stress and antioxidant defenses in goldfish Carassius auratus during anoxia and reoxygenation. Am. J. Physiol. 2001, 280:R100-R107.
    • (2001) Am. J. Physiol. , vol.280
    • Lushchak, V.I.1    Lushchak, L.P.2    Mota, A.A.3    Hermes-Lima, M.4
  • 47
    • 15044342344 scopus 로고    scopus 로고
    • Hypoxia and recovery perturb free radical processes and antioxidant potential in common carp (Cyprinus carpio) tissues
    • Lushchak V.I., Bagnyukova T.V., Lushchak O.V., Storey J.M., Storey K.B. Hypoxia and recovery perturb free radical processes and antioxidant potential in common carp (Cyprinus carpio) tissues. Int. J. Biochem. Cell Biol. 2005, 37:1319-1330.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 1319-1330
    • Lushchak, V.I.1    Bagnyukova, T.V.2    Lushchak, O.V.3    Storey, J.M.4    Storey, K.B.5
  • 49
    • 41349106145 scopus 로고    scopus 로고
    • The effect of potassium dichromate on free radical processes in goldfish: possible protective role of glutathione
    • Lushchak O.V., Kubrak O.I., Nykorak M.Z., Storey K.B., Lushchak V.I. The effect of potassium dichromate on free radical processes in goldfish: possible protective role of glutathione. Aquat. Toxicol. 2008, 87:108-114.
    • (2008) Aquat. Toxicol. , vol.87 , pp. 108-114
    • Lushchak, O.V.1    Kubrak, O.I.2    Nykorak, M.Z.3    Storey, K.B.4    Lushchak, V.I.5
  • 52
    • 0034102513 scopus 로고    scopus 로고
    • The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implication for amyotrophic lateral sclerosis
    • Lyons T.J., Nersissian A., Huang H., Yeom H., Nishida C.R., Graden J.A., Gralla E.B., Valentine J.S. The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implication for amyotrophic lateral sclerosis. J. Biol. Inorg. Chem. 2000, 5:189-203.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 189-203
    • Lyons, T.J.1    Nersissian, A.2    Huang, H.3    Yeom, H.4    Nishida, C.R.5    Graden, J.A.6    Gralla, E.B.7    Valentine, J.S.8
  • 53
    • 0031733563 scopus 로고    scopus 로고
    • Toxicity of cobalt and copper to rainbow trout: application of a mechanistic model for predicting survival
    • Marr J.C.A., Hansen J.A., Meyer J.S., Cacela D., Podrabsky T., Lipton J., Bergman H.L. Toxicity of cobalt and copper to rainbow trout: application of a mechanistic model for predicting survival. Aquat. Toxicol. 1998, 43:225-238.
    • (1998) Aquat. Toxicol. , vol.43 , pp. 225-238
    • Marr, J.C.A.1    Hansen, J.A.2    Meyer, J.S.3    Cacela, D.4    Podrabsky, T.5    Lipton, J.6    Bergman, H.L.7
  • 55
    • 0028170326 scopus 로고
    • Importance of SE-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels C., Raes M., Toussaint O., Remacle J. Importance of SE-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radical Biol. Med. 1994, 17:235-248.
    • (1994) Free Radical Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 56
    • 79960293836 scopus 로고    scopus 로고
    • Hypoxia-induced oxidative DNA damage links with higher level biological effects including specific growth rate in common carp, Cyprinus carpio L. Ecotoxicology. doi:10.1007/s10646-011-0702-5
    • Mustafa, S.A., Sherain, N., Al-Subiai, S.N., Davies, S.J., Jha, A.N., 2011. Hypoxia-induced oxidative DNA damage links with higher level biological effects including specific growth rate in common carp, Cyprinus carpio L. Ecotoxicology. doi:10.1007/s10646-011-0702-5.
    • (2011)
    • Mustafa, S.A.1    Sherain, N.2    Al-Subiai, S.N.3    Davies, S.J.4    Jha, A.N.5
  • 57
    • 0034213330 scopus 로고    scopus 로고
    • A short review on the role of glutathione in the response of yeasts to nutritional, environmental, and oxidative stresses
    • Penninckx M. A short review on the role of glutathione in the response of yeasts to nutritional, environmental, and oxidative stresses. Enzyme Microb. Technol. 2000, 26:737-742.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 737-742
    • Penninckx, M.1
  • 58
    • 0345868849 scopus 로고    scopus 로고
    • Effect of cobalt and chromium ions on bcl-2, bax, caspase-3, and caspase-8 expression in human U937 macrophages
    • Petit A., Mwale F., Zukor D.J., Catelas I., Antoniou J., Huk O.L. Effect of cobalt and chromium ions on bcl-2, bax, caspase-3, and caspase-8 expression in human U937 macrophages. Biomaterials 2004, 25:2013-2018.
    • (2004) Biomaterials , vol.25 , pp. 2013-2018
    • Petit, A.1    Mwale, F.2    Zukor, D.J.3    Catelas, I.4    Antoniou, J.5    Huk, O.L.6
  • 60
    • 0034545719 scopus 로고    scopus 로고
    • Quantification and significance of protein oxidation in biological samples
    • Shacter E. Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 2000, 32:307-326.
    • (2000) Drug Metab. Rev. , vol.32 , pp. 307-326
    • Shacter, E.1
  • 61
    • 0025987977 scopus 로고
    • Oxidative stress: from basic research to clinical application
    • Sies H. Oxidative stress: from basic research to clinical application. Am. J. Med. 1991, 91:31S-38S.
    • (1991) Am. J. Med. , vol.91
    • Sies, H.1
  • 62
    • 0026688511 scopus 로고
    • Iron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
    • Szweda L.I., Stadtman E.R. Iron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. J. Biol. Chem. 1992, 267:3096-3100.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3096-3100
    • Szweda, L.I.1    Stadtman, E.R.2
  • 64
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang G.L., Semenza G.L. Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J. Biol. Chem. 1993, 268:21513-21518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 65
    • 4243935745 scopus 로고
    • Photometric determination of cobalt with nitroso-R-salt
    • Wünsch G. Photometric determination of cobalt with nitroso-R-salt. Talanta 1979, 26:177-179.
    • (1979) Talanta , vol.26 , pp. 177-179
    • Wünsch, G.1
  • 66
    • 0016329173 scopus 로고
    • Effect of cobalt on the synthesis and degradation of hepatic catalase in vivo
    • Yasukochi Y., Nakamura M., Minakami S. Effect of cobalt on the synthesis and degradation of hepatic catalase in vivo. Biochem. J. 1974, 144:455-464.
    • (1974) Biochem. J. , vol.144 , pp. 455-464
    • Yasukochi, Y.1    Nakamura, M.2    Minakami, S.3


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