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Volumn 60, Issue , 2006, Pages 170-180

Catalase: Structure, properties, functions;Katalaza - budowa, włas̈ciwos̈ci, funkcje

Author keywords

Catalase; Functions; Properties; Structure

Indexed keywords

CATALASE; HYDROGEN PEROXIDE;

EID: 33846080254     PISSN: 00325449     EISSN: 17322693     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (104)

References (120)
  • 1
    • 0027505784 scopus 로고
    • Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
    • Adachi S., Nagano S., Ishimori K., Watanabe Y., Morishima I., Egawa T., Kitagawa T., Makino R.: Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase. Biochemistry, 1993; 32: 241-252
    • (1993) Biochemistry , vol.32 , pp. 241-252
    • Adachi, S.1    Nagano, S.2    Ishimori, K.3    Watanabe, Y.4    Morishima, I.5    Egawa, T.6    Kitagawa, T.7    Makino, R.8
  • 3
    • 0018156829 scopus 로고
    • Molecular hybridization in heterozygotes for Swiss-type acatalasemia
    • Aebi H.E., Wyss S.R.: Molecular hybridization in heterozygotes for Swiss-type acatalasemia. Monogr. Hum. Genet., 1978; 10: 200-204
    • (1978) Monogr. Hum. Genet. , vol.10 , pp. 200-204
    • Aebi, H.E.1    Wyss, S.R.2
  • 5
    • 0000286714 scopus 로고
    • Mechanism of oneelectron oxidation of NAD(P)H and function of NADPH bound to catalase
    • Almarsson O., Sinha A., Gopinath E., Bruice T.C.: Mechanism of oneelectron oxidation of NAD(P)H and function of NADPH bound to catalase. J. Am. Chem. Soc., 1993; 115: 7093-7102
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7093-7102
    • Almarsson, O.1    Sinha, A.2    Gopinath, E.3    Bruice, T.C.4
  • 7
    • 0034674055 scopus 로고    scopus 로고
    • Estimation of H2O2 gradients across biomembranes
    • Antunes F., Cadenas E.: Estimation of H2O2 gradients across biomembranes. FEBS Lett., 2000; 475: 121-126
    • (2000) FEBS Lett. , vol.475 , pp. 121-126
    • Antunes, F.1    Cadenas, E.2
  • 8
    • 3042760502 scopus 로고    scopus 로고
    • Properties of catalase-peroxidase lacking its C-terminal domain
    • Baker R.D., Cook C.O., Goodwin D.C.: Properties of catalase-peroxidase lacking its C-terminal domain. Biochem. Biophys. Res. Commun., 2004; 320: 833-839
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 833-839
    • Baker, R.D.1    Cook, C.O.2    Goodwin, D.C.3
  • 9
    • 0003781293 scopus 로고    scopus 로고
    • Wydawnictwo Naukowe PWN, wyd. II, Warszawa
    • Bartosz G.: Druga twarz tlenu. Wydawnictwo Naukowe PWN, wyd. II, Warszawa, 2003
    • (2003) Druga Twarz Tlenu
    • Bartosz, G.1
  • 11
    • 0024199820 scopus 로고
    • Catalases-with and without heme
    • Beyer W.F.Jr., Fridivich I.: Catalases-with and without heme. Basic Life Sci., 1988; 49: 651-661
    • (1988) Basic Life Sci. , vol.49 , pp. 651-661
    • Beyer, W.F.1    Fridivich, I.2
  • 12
    • 70849116316 scopus 로고    scopus 로고
    • Catalase: H2O2: H2O2 oxidoreductase. Reviews on structure and function of catalases
    • eds David Marcey
    • Boon E.M., Downs A., Marcey D.: Catalase: H2O2: H2O2 oxidoreductase. Reviews on structure and function of catalases. In: Biomolecules at Kenyon, eds David Marcey, 1997
    • (1997) Biomolecules at Kenyon
    • Boon, E.M.1    Downs, A.2    Marcey, D.3
  • 13
    • 0030707868 scopus 로고    scopus 로고
    • Basic mechanisms of antioxidant activity
    • Cadenas E.: Basic mechanisms of antioxidant activity. Biofactors, 1997; 6: 391-397
    • (1997) Biofactors , vol.6 , pp. 391-397
    • Cadenas, E.1
  • 16
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A.: Hydroperoxide metabolism in mammalian organs. Physiol. Rev., 1979; 59: 527-605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 17
    • 0043234246 scopus 로고    scopus 로고
    • An electrical potential in the access channel of catalases enhances catalysis
    • Chelikani P., Carpena X., Fita I., Loewen P.C.: An electrical potential in the access channel of catalases enhances catalysis. J. Biol. Chem., 2003; 278: 31290-31296
    • (2003) J. Biol. Chem. , vol.278 , pp. 31290-31296
    • Chelikani, P.1    Carpena, X.2    Fita, I.3    Loewen, P.C.4
  • 18
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • Chelikani P., Fita I., Loewen P.C.: Diversity of structures and properties among catalases. Cell. Mol. Life. Sci., 2004, 61: 192-208
    • (2004) Cell. Mol. Life. Sci. , vol.61 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 19
    • 33947476438 scopus 로고
    • Glutathione peroxidase: The primary agent for elimination of hydrogen peroxide in erythrocytes
    • Cohen G., Hochstein P.: Glutathione peroxidase: The primary agent for elimination of hydrogen peroxide in erythrocytes. Biochemistry, 1963; 2: 1420-1428
    • (1963) Biochemistry , vol.2 , pp. 1420-1428
    • Cohen, G.1    Hochstein, P.2
  • 20
    • 13244271908 scopus 로고    scopus 로고
    • The regulation and role of extracellular glutathione peroxidase
    • Comhair S.A., Erzurun S.C.: The regulation and role of extracellular glutathione peroxidase. Antioxid. Redox Signal., 2005; 7: 72-79
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 72-79
    • Comhair, S.A.1    Erzurun, S.C.2
  • 21
    • 0141537204 scopus 로고    scopus 로고
    • Evaluation of antioxidant status in patients with primary hepatocellular carcinoma
    • Czeczot H., Skrzycki M., Gawryszewska E., Podsiad M., Porembska Z.: Evaluation of antioxidant status in patients with primary hepatocellular carcinoma. Pol. Merk. Lek., 2003; 15: 118-122
    • (2003) Pol. Merk. Lek. , vol.15 , pp. 118-122
    • Czeczot, H.1    Skrzycki, M.2    Gawryszewska, E.3    Podsiad, M.4    Porembska, Z.5
  • 22
    • 13444272195 scopus 로고    scopus 로고
    • Antioxidant status of patients with primary colorectal cancer and liver metastases of colorectal cancer
    • Czeczot H., Skrzycki M., Podsiad M., Gawryszewska E., Nyckowski P., Porembska Z.: Antioxidant status of patients with primary colorectal cancer and liver metastases of colorectal cancer. Pol. Merk. Lek., 2005; 18: 58-61
    • (2005) Pol. Merk. Lek. , vol.18 , pp. 58-61
    • Czeczot, H.1    Skrzycki, M.2    Podsiad, M.3    Gawryszewska, E.4    Nyckowski, P.5    Porembska, Z.6
  • 23
    • 0022980987 scopus 로고
    • Irreversible inactivation of catalase by 3-amino-1,2,4-triazole
    • Darr D., Fridovich I.: Irreversible inactivation of catalase by 3-amino-1,2,4-triazole. Biochem. Pharmacol., 1986; 35: 3642
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 3642
    • Darr, D.1    Fridovich, I.2
  • 24
    • 0030462769 scopus 로고    scopus 로고
    • The peroxisome in retrospect
    • De Duve C.: The peroxisome in retrospect. Ann. N. Y. Acad. Sci., 1996; 804: 1-10
    • (1996) Ann. N. Y. Acad. Sci. , vol.804 , pp. 1-10
    • De Duve, C.1
  • 25
    • 0014819568 scopus 로고
    • Catalase: Physical and chemical properties, mechanism of catalysis, and physical role
    • Deisseroth A., Dounce A.L.: Catalase: physical and chemical properties, mechanism of catalysis, and physical role. Physiol. Rev., 1970; 50: 319-375
    • (1970) Physiol. Rev. , vol.50 , pp. 319-375
    • Deisseroth, A.1    Dounce, A.L.2
  • 26
    • 0001054685 scopus 로고
    • Acatalasemia
    • Scriver CR, Beaudet AL, Sly WS, Valle D, eds, New York: McGraw-Hill, Inc
    • Eaton J.W., Ma M.: Acatalasemia. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds, The Metabolic and Molecular Bases of Inherited Disease. New York: McGraw-Hill, Inc., 1995, 2371-2383
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 2371-2383
    • Eaton, J.W.1    Ma, M.2
  • 27
    • 0032506530 scopus 로고    scopus 로고
    • A hydrogen-producing mitochondrion
    • Embley T.M., Martin W.: A hydrogen-producing mitochondrion. Nature, 1998; 396: 517-519
    • (1998) Nature , vol.396 , pp. 517-519
    • Embley, T.M.1    Martin, W.2
  • 29
    • 0022179287 scopus 로고
    • The active center of catalase
    • Fita I., Rossman M.G.: The active center of catalase. J. Mol. Biol., 1985; 185: 21-37
    • (1985) J. Mol. Biol. , vol.185 , pp. 21-37
    • Fita, I.1    Rossman, M.G.2
  • 31
    • 0018261934 scopus 로고
    • Glutathione peroxidase: Fact and fiction
    • Flohe L.: Glutathione peroxidase: fact and fiction. Ciba Found Symp., 1978, 65: 95-122
    • (1978) Ciba Found Symp. , vol.65 , pp. 95-122
    • Flohe, L.1
  • 32
    • 0030022388 scopus 로고    scopus 로고
    • Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
    • Gaetani G.F., Ferraris A.M., Rolfo M., Mangerini R., Arena S., Kirkman H.N.: Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood, 1996; 87: 1595-1599
    • (1996) Blood , vol.87 , pp. 1595-1599
    • Gaetani, G.F.1    Ferraris, A.M.2    Rolfo, M.3    Mangerini, R.4    Arena, S.5    Kirkman, H.N.6
  • 33
    • 0027129196 scopus 로고
    • Two cases of acatalasemia in Hungary
    • Goth L.: Two cases of acatalasemia in Hungary. Clin. Chim. Acta, 1992; 207: 155-158
    • (1992) Clin. Chim. Acta , vol.207 , pp. 155-158
    • Goth, L.1
  • 34
    • 0343923639 scopus 로고    scopus 로고
    • Further genetic heterogeneity in acatalasemia
    • Goth L.: Further genetic heterogeneity in acatalasemia. Electrophoresis, 1997; 18: 1942-1943
    • (1997) Electrophoresis , vol.18 , pp. 1942-1943
    • Goth, L.1
  • 35
    • 0345294370 scopus 로고    scopus 로고
    • Genetic heterogeneity of the 5' uncoding region of the catalase gene in Hungarian acatalasemic and hypocatalasemic subjects
    • Goth L.: Genetic heterogeneity of the 5' uncoding region of the catalase gene in Hungarian acatalasemic and hypocatalasemic subjects. Clin. Chim. Acta, 1998; 271: 73-78
    • (1998) Clin. Chim. Acta , vol.271 , pp. 73-78
    • Goth, L.1
  • 36
    • 0034976899 scopus 로고    scopus 로고
    • A new type of inherited catalase deficiencies: Its characterization and comparison to the Japanese and Swiss type of acatalasemia
    • Goth L.: A new type of inherited catalase deficiencies: its characterization and comparison to the Japanese and Swiss type of acatalasemia. Blood Cells Mol. Dis., 2001; 27: 512-517
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 512-517
    • Goth, L.1
  • 37
    • 0035949765 scopus 로고    scopus 로고
    • A novel catalase mutation (a G insertion in exon 2) causes the type B of the Hungarian acatalasemia
    • Goth L.: A novel catalase mutation (a G insertion in exon 2) causes the type B of the Hungarian acatalasemia. Clin. Chim. Acta, 2001; 311: 161-163
    • (2001) Clin. Chim. Acta , vol.311 , pp. 161-163
    • Goth, L.1
  • 38
    • 0027818788 scopus 로고
    • Further characterisation of Hungarian acatalasemia by Hinf1 polymorphism of catalase gene
    • Goth L., Alizadeh B.N., Sussman H.H.: Further characterisation of Hungarian acatalasemia by Hinf1 polymorphism of catalase gene. Enzyme Protein, 1993; 47: 156-159
    • (1993) Enzyme Protein , vol.47 , pp. 156-159
    • Goth, L.1    Alizadeh, B.N.2    Sussman, H.H.3
  • 39
    • 0034715982 scopus 로고    scopus 로고
    • Hereditary catalase deficiencies and increased risk of diabetes
    • Goth L., Eaton J.W.: Hereditary catalase deficiencies and increased risk of diabetes. Lancet, 2000; 356: 1820-1821
    • (2000) Lancet , vol.356 , pp. 1820-1821
    • Goth, L.1    Eaton, J.W.2
  • 40
    • 0033885802 scopus 로고    scopus 로고
    • A simple PCR-heteroduplex screening method for detection of a common mutation of the catalase gene in Hungary
    • Goth L., Gorzsas A., Kalmar T.: A simple PCR-heteroduplex screening method for detection of a common mutation of the catalase gene in Hungary. Clin. Chem., 2000; 46: 1199-1200
    • (2000) Clin. Chem. , vol.46 , pp. 1199-1200
    • Goth, L.1    Gorzsas, A.2    Kalmar, T.3
  • 41
    • 0035490106 scopus 로고    scopus 로고
    • Blood catalase deficiency and diabetes in Hungary
    • Goth L., Lenkey A., Bigler W.N.: Blood catalase deficiency and diabetes in Hungary. Diabetes Care, 2001; 24: 1839-1840
    • (2001) Diabetes Care , vol.24 , pp. 1839-1840
    • Goth, L.1    Lenkey, A.2    Bigler, W.N.3
  • 42
    • 0035165555 scopus 로고    scopus 로고
    • A novel catalase mutation detected by polymerase chain reaction-single strand conformation polymorphism, nucleotide sequencing, and western blot analyses is responsible for the type C of Hungarian acatalasemia
    • Goth L., Rass P., Madarasi I.: A novel catalase mutation detected by polymerase chain reaction-single strand conformation polymorphism, nucleotide sequencing, and western blot analyses is responsible for the type C of Hungarian acatalasemia. Electrophoresis, 2001; 22: 49-51
    • (2001) Electrophoresis , vol.22 , pp. 49-51
    • Goth, L.1    Rass, P.2    Madarasi, I.3
  • 43
    • 16344389174 scopus 로고    scopus 로고
    • Catalase enzyme mutations and their association with diseases
    • Goth L., Rass P., Pay A.: Catalase enzyme mutations and their association with diseases. Mol. Diagn., 2004; 8: 141-149
    • (2004) Mol. Diagn. , vol.8 , pp. 141-149
    • Goth, L.1    Rass, P.2    Pay, A.3
  • 44
    • 0343192414 scopus 로고    scopus 로고
    • A novel catalase mutation (a GA insertion) causes the Hungarian type of acatalasemia
    • Goth L., Shemirani A., Kalmar T.: A novel catalase mutation (a GA insertion) causes the Hungarian type of acatalasemia. Blood Cells Mol. Dis., 2000; 26: 151-154
    • (2000) Blood Cells Mol. Dis. , vol.26 , pp. 151-154
    • Goth, L.1    Shemirani, A.2    Kalmar, T.3
  • 45
    • 0141749475 scopus 로고    scopus 로고
    • The effects of hydrogen peroxide promoted by homocysteine and inherited catalase deficiency on human hypocatalasemic patients
    • Goth L., Vitai M.: The effects of hydrogen peroxide promoted by homocysteine and inherited catalase deficiency on human hypocatalasemic patients. Free Radic. Biol. Med., 2003; 35: 882-888
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 882-888
    • Goth, L.1    Vitai, M.2
  • 46
    • 18844424909 scopus 로고    scopus 로고
    • Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus
    • Goth L., Vitai M., Rass P., Sukei E., Pay A.: Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus. Electrophoresis, 2005; 26: 1646-1649
    • (2005) Electrophoresis , vol.26 , pp. 1646-1649
    • Goth, L.1    Vitai, M.2    Rass, P.3    Sukei, E.4    Pay, A.5
  • 47
    • 0026322413 scopus 로고
    • Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood
    • Guemouri L., Artur Y., Herbeth B., Jeandel C., Cuny G., Siest G.: Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood. Clin. Chem., 1991; 37: 1932-1937
    • (1991) Clin. Chem. , vol.37 , pp. 1932-1937
    • Guemouri, L.1    Artur, Y.2    Herbeth, B.3    Jeandel, C.4    Cuny, G.5    Siest, G.6
  • 50
    • 75449134009 scopus 로고
    • Genetic heterogeneity in human acatalasia
    • Hamilton H.B.; Neel J.V.: Genetic heterogeneity in human acatalasia. Am. J. Hum. Genet., 1963, 15: 408-419
    • (1963) Am. J. Hum. Genet. , vol.15 , pp. 408-419
    • Hamilton, H.B.1    Neel, J.V.2
  • 51
    • 73049138328 scopus 로고
    • The frequency in Japan of carriers of the rare 'recessive' gene causing acatalasemia
    • Hamilton H.B., Neel J.V., Kobara T.Y., Ozaki K.: The frequency in Japan of carriers of the rare 'recessive' gene causing acatalasemia. J. Clin. Invest., 1961; 40: 2199-2208
    • (1961) J. Clin. Invest. , vol.40 , pp. 2199-2208
    • Hamilton, H.B.1    Neel, J.V.2    Kobara, T.Y.3    Ozaki, K.4
  • 52
    • 0035956672 scopus 로고    scopus 로고
    • Catalase deficiency, diabetes and mitochondrial function
    • Heales S.J.R.: Catalase deficiency, diabetes and mitochondrial function. Lancet, 2001; 357: 314
    • (2001) Lancet , vol.357 , pp. 314
    • Heales, S.J.R.1
  • 53
    • 0028364445 scopus 로고
    • NADPH binding and control of catalase compound II formation: Comparison of bovine, yeast and Escherichia coli enzymes
    • Hillar A., Nicholls P, Switala J., Loewen P.C.: NADPH binding and control of catalase compound II formation: comparison of bovine, yeast and Escherichia coli enzymes. Biochem. J., 1994; 300: 531-539
    • (1994) Biochem. J. , vol.300 , pp. 531-539
    • Hillar, A.1    Nicholls, P.2    Switala, J.3    Loewen, P.C.4
  • 54
    • 0028339178 scopus 로고
    • Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by non-radioisotopic single-strand conformation polymorphism (SSCP) analysis
    • Hirono A, Miwa S, Fujii H, Ishida F, Yamada K, Kubota K.: Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by non-radioisotopic single-strand conformation polymorphism (SSCP) analysis. Blood, 1994; 83: 3363-3368
    • (1994) Blood , vol.83 , pp. 3363-3368
    • Hirono, A.1    Miwa, S.2    Fujii, H.3    Ishida, F.4    Yamada, K.5    Kubota, K.6
  • 56
    • 0025881009 scopus 로고
    • Developmental immunohistochemistry of catalase in the human brain
    • Houdou S., Kuruta A., Hasegawa M.: Developmental immunohistochemistry of catalase in the human brain. Brain Res., 1991; 556: 267-270
    • (1991) Brain Res. , vol.556 , pp. 267-270
    • Houdou, S.1    Kuruta, A.2    Hasegawa, M.3
  • 57
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J.A., Chin S.M., Linn S.: Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science, 1988; 240: 640-642
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 59
    • 0035802360 scopus 로고    scopus 로고
    • Theoretical study of the mechanisms of substrate recognition by catalase
    • Kalko S.G., Gelpi J.L., Fita I., Orozco M.: Theoretical study of the mechanisms of substrate recognition by catalase. J. Am. Chem. Soc., 2001; 123: 9665-9672
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9665-9672
    • Kalko, S.G.1    Gelpi, J.L.2    Fita, I.3    Orozco, M.4
  • 60
    • 0009424743 scopus 로고
    • Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH
    • Kirkman H.N., Gaetani G.F.: Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci., 1984; 81: 4343-4347
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 4343-4347
    • Kirkman, H.N.1    Gaetani, G.F.2
  • 61
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry
    • Kirkman H.N., Rolfo M., Ferraris A.M., Gaetani G.F.: Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. J. Biol. Chem., 1999, 274, 13908-13914
    • (1999) J. Biol. Chem. , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 62
    • 0026544886 scopus 로고
    • Detection of a common mutation of the catalase gene in Japanese acatalasemic patients
    • Kishimoto Y., Murakami Y., Hayashi K., Takahara S., Sugimura T., Sekiya T.: Detection of a common mutation of the catalase gene in Japanese acatalasemic patients. Hum. Genet., 1992; 88: 487-490
    • (1992) Hum. Genet. , vol.88 , pp. 487-490
    • Kishimoto, Y.1    Murakami, Y.2    Hayashi, K.3    Takahara, S.4    Sugimura, T.5    Sekiya, T.6
  • 64
    • 0030854046 scopus 로고    scopus 로고
    • Phylogenetic relationships among prokaryotic and eukaryotic catalases
    • Klotz M., Klassen G., Loewen P.: 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.1    Klassen, G.2    Loewen, P.3
  • 66
    • 0021746044 scopus 로고
    • Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA
    • Korneluk R.G., Quan F., Lewis W.H., Guise K.S., Willard H.F., Holmes M.T., Gravel R.A.: Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. J. Biol. Chem., 1984; 259: 13819-13823
    • (1984) J. Biol. Chem. , vol.259 , pp. 13819-13823
    • Korneluk, R.G.1    Quan, F.2    Lewis, W.H.3    Guise, K.S.4    Willard, H.F.5    Holmes, M.T.6    Gravel, R.A.7
  • 68
    • 0024153342 scopus 로고
    • Oxygen toxicity. I. Damage of living cells
    • Liczmański A.E.: Oxygen toxicity. I. Damage of living cells. Post. Biochem., 1988, 34: 273-291
    • (1988) Post. Biochem. , vol.34 , pp. 273-291
    • Liczmański, A.E.1
  • 69
    • 2642617823 scopus 로고    scopus 로고
    • Oxidation of catalase by singlet oxygen
    • Lledías F., Rangel P., Hansberg W.: Oxidation of catalase by singlet oxygen. J. Biol. Chem., 1998; 273: 10630-10637
    • (1998) J. Biol. Chem. , vol.273 , pp. 10630-10637
    • Lledías, F.1    Rangel, P.2    Hansberg, W.3
  • 70
    • 0037774042 scopus 로고
    • Physiological studies of Connecticut leaf tobacco
    • Loew O.: Physiological studies of Connecticut leaf tobacco. U.S. Dept. Agri. Repts., 1900; 65: 5-57
    • (1900) U.S. Dept. Agri. Repts. , vol.65 , pp. 5-57
    • Loew, O.1
  • 71
    • 0003119571 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Loewen P.C.: Bacterial catalases. Cold Spring Harbor Laboratory Press, 1997, Cold Spring Harbor, NY
    • (1997) Bacterial Catalases
    • Loewen, P.C.1
  • 73
    • 0001866321 scopus 로고    scopus 로고
    • Catalase-an "old" enzyme that continues to surprise us
    • Loewen P.C., Klotz M.G., Hassett D.J.: Catalase-an "old" enzyme that continues to surprise us. ASM News., 2000; 66: 76-82
    • (2000) ASM News. , vol.66 , pp. 76-82
    • Loewen, P.C.1    Klotz, M.G.2    Hassett, D.J.3
  • 74
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R.: Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med., 1997; 23: 134-147
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 76
    • 0029832625 scopus 로고    scopus 로고
    • Identification of a novel growthpromoting factor with a wide target cell spectrum from various tumor cells as catalase
    • Miyamoto T., Hayashi M., Takeuchi A., Okamoto T., Kawashima S., Takii T., Hayashi H., Onozaki K.: Identification of a novel growthpromoting factor with a wide target cell spectrum from various tumor cells as catalase. J. Biochem., 1996; 120: 725-730
    • (1996) J. Biochem. , vol.120 , pp. 725-730
    • Miyamoto, T.1    Hayashi, M.2    Takeuchi, A.3    Okamoto, T.4    Kawashima, S.5    Takii, T.6    Hayashi, H.7    Onozaki, K.8
  • 77
    • 0031441273 scopus 로고    scopus 로고
    • Direct evidence for catalase as the predominant H2O2-removing enzyme in human erythrocytes
    • Mueller S., Riedel H.D., Stremmel W.: Direct evidence for catalase as the predominant H2O2-removing enzyme in human erythrocytes. Blood, 1997; 90: 4973-4978
    • (1997) Blood , vol.90 , pp. 4973-4978
    • Mueller, S.1    Riedel, H.D.2    Stremmel, W.3
  • 80
    • 0019977295 scopus 로고
    • Chromosome abnormalities involving 11p13 and low erythrocyte catalase activity
    • Niikawa N., Fukushima Y., Taniguchi N., Iizuka S., Kajii T.: Chromosome abnormalities involving 11p13 and low erythrocyte catalase activity. Hum. Genet., 1982; 60: 373-375
    • (1982) Hum. Genet. , vol.60 , pp. 373-375
    • Niikawa, N.1    Fukushima, Y.2    Taniguchi, N.3    Iizuka, S.4    Kajii, T.5
  • 81
    • 0026101082 scopus 로고
    • Acatalasemia
    • Ogata M.: Acatalasemia. Hum. Genet., 1991; 86: 331-340
    • (1991) Hum. Genet. , vol.86 , pp. 331-340
    • Ogata, M.1
  • 84
    • 0021681841 scopus 로고
    • Catalase: An old enzyme with a new role?
    • Percy M.E.: Catalase: an old enzyme with a new role? Can. J. Biochem. Cell Biol., 1984; 62: 1006-1014
    • (1984) Can. J. Biochem. Cell Biol. , vol.62 , pp. 1006-1014
    • Percy, M.E.1
  • 85
    • 0017080971 scopus 로고
    • Nucleotide sequences of globin messenger RNA
    • Proudfoot N.J., Brownlee G.G.: Nucleotide sequences of globin messenger RNA. Br. Med. Bull., 1976; 32: 251-256
    • (1976) Br. Med. Bull. , vol.32 , pp. 251-256
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 86
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A.: Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol., 2000; 296: 295-309
    • (2000) J. Mol. Biol. , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 88
  • 89
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., Beckman J.S., Bush K.M., Freeman B.A.: Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem., 1991; 266: 4244-4250
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 91
    • 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 S.G., Yang K.S., Kang S.W., Woo H.A., Chang T.S.: Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid. Redox Signal., 2005; 7: 619-626
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 619-626
    • Rhee, S.G.1    Yang, K.S.2    Kang, S.W.3    Woo, H.A.4    Chang, T.S.5
  • 92
    • 0042070083 scopus 로고
    • Cytoplasmic catalase: Cytochemistry and physiology
    • Roels F., Geerts A.: Cytoplasmic catalase: cytochemistry and. Physiology. Ann. NY Acad. Sci., 1982; 386: 534-536
    • (1982) Ann. NY Acad. Sci. , vol.386 , pp. 534-536
    • Roels, F.1    Geerts, A.2
  • 93
    • 0035176642 scopus 로고    scopus 로고
    • Structure of tetragonal crystals of human erythrocyte catalase Acta Crystallogr
    • Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P.: Structure of tetragonal crystals of human erythrocyte catalase Acta Crystallogr. D. Biol. Crystallogr., 2001; 57: 1-7
    • (2001) D. Biol. Crystallogr. , vol.57 , pp. 1-7
    • Safo, M.K.1    Musayev, F.N.2    Wu, S.H.3    Abraham, D.J.4    Ko, T.P.5
  • 94
    • 28544434692 scopus 로고    scopus 로고
    • Prevention of apoptosis as a possible mechanism behind improved cryoprotection of hematopoietic cells by catalase and trehalose
    • Sasnoor L.M., Kale V.P., Limaye L.S.: Prevention of apoptosis as a possible mechanism behind improved cryoprotection of hematopoietic cells by catalase and trehalose. Transplantation, 2005; 80: 1251-1260
    • (2005) Transplantation , vol.80 , pp. 1251-1260
    • Sasnoor, L.M.1    Kale, V.P.2    Limaye, L.S.3
  • 97
    • 77956932249 scopus 로고
    • Catalase
    • 3rd edn. (Boyer PD, ed). New. York: Academic Press
    • Schonbaum G.R., Chance B.: Catalase. In: The. Enzymes, Vol. 13, 3rd edn. (Boyer PD, ed). New. York: Academic Press, 1976; 363-408
    • (1976) The. Enzymes , vol.13 , pp. 363-408
    • Schonbaum, G.R.1    Chance, B.2
  • 98
    • 0023224132 scopus 로고
    • Localization of the human catalase and apolipoprotein A-I genes to chromosome 11
    • Schroeder W.T., Saunders G. F.: Localization of the human catalase and apolipoprotein A-I genes to chromosome 11. Cytogenet. Cell Genet., 1987; 44: 231-233
    • (1987) Cytogenet. Cell Genet. , vol.44 , pp. 231-233
    • Schroeder, W.T.1    Saunders, G.F.2
  • 99
    • 0026332035 scopus 로고
    • Does hydrogen peroxide exist 'free' in biological systems?
    • Schubert J., Wilmer J.W.: Does hydrogen peroxide exist 'free' in biological systems? Free Radic. Biol. Med., 1991; 11: 545-555
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 545-555
    • Schubert, J.1    Wilmer, J.W.2
  • 100
    • 0016123046 scopus 로고
    • Biochemistry of the peroxisome in the liver cell
    • Sies H.: Biochemistry of the peroxisome in the liver cell. Angew. Chem. Int. Ed. Engl. 1974, 13: 706-718
    • (1974) Angew. Chem. Int. Ed. Engl. , vol.13 , pp. 706-718
    • Sies, H.1
  • 101
    • 0030894162 scopus 로고    scopus 로고
    • Oxidative stress: Oxidants and antioxidants
    • Sies H.: Oxidative stress: oxidants and antioxidants. Exp. Physiol., 1997; 82: 291-295
    • (1997) Exp. Physiol. , vol.82 , pp. 291-295
    • Sies, H.1
  • 102
    • 0030477745 scopus 로고    scopus 로고
    • Mammalian peroxisomes: Metabolism of oxygen and reactive oxygen species
    • Singh I.: Mammalian peroxisomes: metabolism of oxygen and reactive oxygen species. Ann. N. Y. Acad. Sci., 1996; 804: 612-627
    • (1996) Ann. N. Y. Acad. Sci. , vol.804 , pp. 612-627
    • Singh, I.1
  • 103
    • 0027164510 scopus 로고
    • Cells enriched for catalase are sensitized to the toxicities of bleomycin, adriamycin, and paraquat
    • Speranza M., Bagley A.C., Lynch R.E.: Cells enriched for catalase are sensitized to the toxicities of bleomycin, adriamycin, and paraquat. J. Biol. Chem. 1993; 268: 19039-19043
    • (1993) J. Biol. Chem. , vol.268 , pp. 19039-19043
    • Speranza, M.1    Bagley, A.C.2    Lynch, R.E.3
  • 106
    • 0028477250 scopus 로고
    • Catalase activity of chloroperoxidase and its interaction with peroxidase activity
    • Sun W., Kadima T.A., Pickard M.A., Dunford H.B.: Catalase activity of chloroperoxidase and its interaction with peroxidase activity. Biochem. Cell. Biol., 1994; 72: 321-331
    • (1994) Biochem. Cell. Biol. , vol.72 , pp. 321-331
    • Sun, W.1    Kadima, T.A.2    Pickard, M.A.3    Dunford, H.B.4
  • 107
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes, and carcinogenesis
    • Sun Y.: Free radicals, antioxidant enzymes, and carcinogenesis. Free Radic. Biol. Med., 1990; 8: 583-599
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 583-599
    • Sun, Y.1
  • 108
    • 0037095620 scopus 로고    scopus 로고
    • Diversity of properties among catalases
    • Switala J., Loewen P.C.: Diversity of properties among catalases. Arch. Biochem. Biophys., 2002; 401: 145-154
    • (2002) Arch. Biochem. Biophys. , vol.401 , pp. 145-154
    • Switala, J.1    Loewen, P.C.2
  • 109
    • 0000296829 scopus 로고
    • Progressive oral gangrene, probably due to lack of catalase in blood (acatalasema): Report of nine cases
    • Takahara S.: Progressive oral gangrene, probably due to lack of catalase in blood (acatalasema): report of nine cases. Lancet., 1952; 11: 1101-1104
    • (1952) Lancet. , vol.11 , pp. 1101-1104
    • Takahara, S.1
  • 110
    • 0038236523 scopus 로고    scopus 로고
    • Structurefunction study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression
    • Ueda M., Kinoshita H., Maeda S.I., Zou W., Tanaka A.: Structurefunction study of the amino-terminal stretch of the catalase subunit molecule in oligomerization, heme binding, and activity expression. Appl. Microbiol. Biotechnol., 2003; 61: 488-494
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 488-494
    • Ueda, M.1    Kinoshita, H.2    Maeda, S.I.3    Zou, W.4    Tanaka, A.5
  • 112
    • 0342981766 scopus 로고    scopus 로고
    • Reference ranges of normal blood catalase activity and levels in familial hypocatalasemia in Hungary
    • Vitai M., Goth L.: Reference ranges of normal blood catalase activity and levels in familial hypocatalasemia in Hungary. Clin. Chim. Acta., 1997; 261: 35-42
    • (1997) Clin. Chim. Acta. , vol.261 , pp. 35-42
    • Vitai, M.1    Goth, L.2
  • 113
    • 0027167719 scopus 로고
    • Molecular evolutionary analysis based on the amino acid sequence of catalase
    • von Ossowski I., Hausner G., Loewen P.C.: Molecular evolutionary analysis based on the amino acid sequence of catalase. J. Mol. Evol., 1993; 37: 71-76
    • (1993) J. Mol. Evol. , vol.37 , pp. 71-76
    • Von Ossowski, I.1    Hausner, G.2    Loewen, P.C.3
  • 114
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G.: Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol., 1992; 2: 388-393
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 115
    • 0025156747 scopus 로고
    • Molecular analysis of human acatalasemia: Identification of a splicing mutation
    • Wen J.K., Osumi T., Hashimoto T., Ogata M.: Molecular analysis of human acatalasemia: identification of a splicing mutation. J. Molec. Biol., 1990; 211: 383-393
    • (1990) J. Molec. Biol. , vol.211 , pp. 383-393
    • Wen, J.K.1    Osumi, T.2    Hashimoto, T.3    Ogata, M.4
  • 116
    • 0018819411 scopus 로고
    • Assignment of the gene coding for human catalase to the short arm of chromosome 11
    • Wieacker P., Mueller C.R., Mayerova A., Grzeschik K.H., Ropers H.H.: Assignment of the gene coding for human catalase to the short arm of chromosome 11. Ann. Genet., 1980, 23: 73-77
    • (1980) Ann. Genet. , vol.23 , pp. 73-77
    • Wieacker, P.1    Mueller, C.R.2    Mayerova, A.3    Grzeschik, K.H.4    Ropers, H.H.5
  • 117
    • 0032924755 scopus 로고    scopus 로고
    • Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu,Znsuperoxide dismutase and catalase
    • Yabuki M., Kariya S., Ishisaka R., Yasuda T., Yoshioka T., Horton A.A., Utsumi K.: Resistance to nitric oxide-mediated apoptosis in HL-60 variant cells is associated with increased activities of Cu,Znsuperoxide dismutase and catalase. Free Radic. Biol. Med., 1999; 26: 325-332
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 325-332
    • Yabuki, M.1    Kariya, S.2    Ishisaka, R.3    Yasuda, T.4    Yoshioka, T.5    Horton, A.A.6    Utsumi, K.7
  • 118
    • 0023988178 scopus 로고
    • Catalase in Guinea-pig hepatocytes in localised in cytoplasm, nuclear matrix and peroxisomes
    • Yamamoto K., Volkl A., Hashimoto T., Fahimi H.D.: Catalase in guinea-pig hepatocytes in localised in cytoplasm, nuclear matrix and peroxisomes. Eur. J. Cell Biol., 1988; 46: 129-135
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 129-135
    • Yamamoto, K.1    Volkl, A.2    Hashimoto, T.3    Fahimi, H.D.4
  • 119
    • 0028892421 scopus 로고
    • Serum catalase as marker of graft-vs-host disease in allogeneic bone marrow transplant recipients: Pilot study
    • Yasmineh W.G., Kaur T.P., Blazar B.R., Theologides A.: Serum catalase as marker of graft-vs-host disease in allogeneic bone marrow transplant recipients: pilot study. Clin. Chem., 1995; 41: 1574-1580
    • (1995) Clin. Chem. , vol.41 , pp. 1574-1580
    • Yasmineh, W.G.1    Kaur, T.P.2    Blazar, B.R.3    Theologides, A.4
  • 120
    • 0038360689 scopus 로고    scopus 로고
    • Understanding the structure and function of catalases: Clues from molecular evolution and in vitro mutagenesis
    • Zamocky M., Koller F.: Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol., 1999; 72: 19-66
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 19-66
    • Zamocky, M.1    Koller, F.2


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