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Volumn 48, Issue 6, 2000, Pages 2092-2096

Cloning and expression of a cDNA coding for catalase from zebrafish (Danio rerio)

Author keywords

Catalase; CDNA; Danio rerio; Escherichia coli; Expression; Molecular cloning; PET 20b(+); RACE PCR; Zebrafish

Indexed keywords

CATALASE; COMPLEMENTARY DNA; RECOMBINANT PROTEIN;

EID: 0033936557     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf990838+     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi, H. Catalase in vitro. Methods Enzymol. 1984, 105, 121-126.
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 0000635752 scopus 로고
    • Catalase, glutathione peroxidase and superoxide dismutase in different fish species
    • Aksnes, A.; Njaa, L. R. Catalase, glutathione peroxidase and superoxide dismutase in different fish species. Comp. Biochem. Physiol. 1981, 69B, 893-896.
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 893-896
    • Aksnes, A.1    Njaa, L.R.2
  • 3
  • 4
    • 0028907003 scopus 로고
    • A 3′ untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69-kDa redox-sensitive protein
    • Clerch, L. B. A 3′ untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69-kDa redox-sensitive protein. Arch. Biochem. Biophys. 1995, 317, 267-274.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 267-274
    • Clerch, L.B.1
  • 5
    • 0014819568 scopus 로고
    • Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role
    • Deisseroth, A.; Dounce, A. L. Catalase: physical and chemical properties, mechanism of catalysis, and physiological role. Physiol. Rev. 1970, 50, 319-375.
    • (1970) Physiol. Rev. , vol.50 , pp. 319-375
    • Deisseroth, A.1    Dounce, A.L.2
  • 7
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman, D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 1956, 11, 298-300.
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 8
    • 0008440291 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA coding for copper/zinc-superoxide dismutase from zebrafish and its expression in Escherichia coli
    • Ken, C. F.; Shaw, J. F.; Wu, J. L.; Lin, C. T. Molecular cloning of a cDNA coding for copper/zinc-superoxide dismutase from zebrafish and its expression in Escherichia coli. J. Agric. Food Chem. 1998, 46, 2863-2867.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2863-2867
    • Ken, C.F.1    Shaw, J.F.2    Wu, J.L.3    Lin, C.T.4
  • 9
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz, M. G.; Klassen, G. R.; Loewen, P. C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol. Biol. Evol. 1997, 14, 951-958.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 951-958
    • Klotz, M.G.1    Klassen, G.R.2    Loewen, P.C.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structure protein during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structure protein during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0023002263 scopus 로고
    • Antioxidant enzyme activities and malondialdehyde, glutathione and methemoglobin concentration in channel catfish exposed to DFF and N-butylmercaptan
    • Mather-Mihaich, E.; Diguilio, R. T. Antioxidant enzyme activities and malondialdehyde, glutathione and methemoglobin concentration in channel catfish exposed to DFF and N-butylmercaptan. Comp. Biochem. Physiol. 1986, 85C, 427-432.
    • (1986) Comp. Biochem. Physiol. , vol.85 C , pp. 427-432
    • Mather-Mihaich, E.1    Diguilio, R.T.2
  • 14
    • 0024804437 scopus 로고
    • Effect of chronic mercuric chloride exposure on liver and muscle enzymes in fish
    • Nicholls, D. M.; Teichert-Kuliszewska, K.; Girgis, G. R. Effect of chronic mercuric chloride exposure on liver and muscle enzymes in fish. Comp. Biochem. Physiol. 1989, 94C, 265-270.
    • (1989) Comp. Biochem. Physiol. , vol.94 C , pp. 265-270
    • Nicholls, D.M.1    Teichert-Kuliszewska, K.2    Girgis, G.R.3
  • 15
    • 0025294383 scopus 로고
    • cDNA and deduced amino acid sequence of Drosophila catalase
    • Orr, E. C.; Bewley, G. C.; Orr, W. C. cDNA and deduced amino acid sequence of Drosophila catalase. Nucleic Acids Res. 1990, 18, 3663.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3663
    • Orr, E.C.1    Bewley, G.C.2    Orr, W.C.3
  • 16
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr, W. C.; Sohal, R. S. Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 1994, 263, 1128-1130.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 17
    • 0029619096 scopus 로고
    • Oxidative stress in fish exposed to model xenobiotics. Oxidatively modified forms of Cu, Zn-superoxide dismutase as potential biomarkers
    • Pedrajas, J. R.; Peinado, J.; Lopez-Barea, J. Oxidative stress in fish exposed to model xenobiotics. Oxidatively modified forms of Cu, Zn-superoxide dismutase as potential biomarkers. Chem.-Biol. Interact. 1995, 98, 267-282.
    • (1995) Chem.-Biol. Interact. , vol.98 , pp. 267-282
    • Pedrajas, J.R.1    Peinado, J.2    Lopez-Barea, J.3
  • 18
    • 0022599598 scopus 로고
    • Isolation and characterization of the human catalase gene
    • Quan, F.; Korneluk, R. G.; Tropak, M. B.; Gravel, R. A. Isolation and characterization of the human catalase gene. Nucleic Acids Res. 1986, 14, 5321-5335.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5321-5335
    • Quan, F.1    Korneluk, R.G.2    Tropak, M.B.3    Gravel, R.A.4
  • 19
    • 0023933464 scopus 로고
    • Effects of metal ions on the antioxidant enzyme activities, protein contents and lipid peroxidation of carp tissues
    • Radi, A. A. R.; Marcovics, B. Effects of metal ions on the antioxidant enzyme activities, protein contents and lipid peroxidation of carp tissues. Comp. Biochem. Physiol. 1988, 90C, 69-72.
    • (1988) Comp. Biochem. Physiol. , vol.90 C , pp. 69-72
    • Radi, A.A.R.1    Marcovics, B.2
  • 20
    • 0028217916 scopus 로고
    • Complete cDNA and 5′ genomic sequences and multilevel regulation of the mouse catalase gene
    • Reimer, D. L.; Bailley, J.; Singh, S. M. Complete cDNA and 5′ genomic sequences and multilevel regulation of the mouse catalase gene. Genomics 1994, 21, 325-336.
    • (1994) Genomics , vol.21 , pp. 325-336
    • Reimer, D.L.1    Bailley, J.2    Singh, S.M.3
  • 21
    • 0029656230 scopus 로고    scopus 로고
    • Fish blood parameters as a potential tool for identification of stress caused by environmental factors and chemical intoxication
    • Roche, H.; Boge, G. Fish blood parameters as a potential tool for identification of stress caused by environmental factors and chemical intoxication. Mar. Environ. Res. 1996, 41, 27-43.
    • (1996) Mar. Environ. Res. , vol.41 , pp. 27-43
    • Roche, H.1    Boge, G.2
  • 23
    • 0025004552 scopus 로고
    • Nucleotide and deduced amino acid sequences of mouse catalase: Molecular analysis of a low activity mutant
    • Shaffer, J. B.; Preston, K. E.; Shepard, B. A. Nucleotide and deduced amino acid sequences of mouse catalase: molecular analysis of a low activity mutant. Nucleic Acids Res. 1990, 18, 4941.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4941
    • Shaffer, J.B.1    Preston, K.E.2    Shepard, B.A.3
  • 24
    • 0028298660 scopus 로고
    • Combined effect of zinc and lead on the hepatic superoxide dismutase-catalase system in carp (Cyprinus carpio)
    • St. Dimitrova, M.; Tishinova, V.; Velcheva, V. Combined effect of zinc and lead on the hepatic superoxide dismutase-catalase system in carp (Cyprinus carpio). Comp. Biochem. Physiol. 1994, 108C, 43-46.
    • (1994) Comp. Biochem. Physiol. , vol.108 C , pp. 43-46
    • St. Dimitrova, M.1    Tishinova, V.2    Velcheva, V.3
  • 25
    • 0023050076 scopus 로고
    • A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels
    • Wayne, L. G.; Diaz, G. A. A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal. Biochem. 1986, 157, 89-92.
    • (1986) Anal. Biochem. , vol.157 , pp. 89-92
    • Wayne, L.G.1    Diaz, G.A.2
  • 26
    • 33646801477 scopus 로고
    • Comparative studies on superoxide dismutase, catalase and peroxidase levels in erthrocytes and livers of different freshwater and marine fish species
    • Wdzieczak, J.; Zalesna, G.; Wujec, A.; Peres, G. Comparative studies on superoxide dismutase, catalase and peroxidase levels in erthrocytes and livers of different freshwater and marine fish species. Comp. Biochem. Physiol. 1982, 73B, 361-365.
    • (1982) Comp. Biochem. Physiol. , vol.73 B , pp. 361-365
    • Wdzieczak, J.1    Zalesna, G.2    Wujec, A.3    Peres, G.4
  • 27
    • 0021237391 scopus 로고
    • Comparative studies on superoxide dismutase and catalase in livers of fish and other Antarctic vertebrates
    • Witas, H.; Gabryelak, T.; Matkovics, B. Comparative studies on superoxide dismutase and catalase in livers of fish and other Antarctic vertebrates. Comp. Biochem. Physiol. 1984, 77C, 409-411.
    • (1984) Comp. Biochem. Physiol. , vol.77 C , pp. 409-411
    • Witas, H.1    Gabryelak, T.2    Matkovics, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.