메뉴 건너뛰기




Volumn 44, Issue 1, 1999, Pages 32-36

Purification and identification of the type of superoxide dismutase from Glœocapsa sp

Author keywords

[No Author keywords available]

Indexed keywords

GLOEOCAPSA;

EID: 0040194004     PISSN: 00155632     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02816217     Document Type: Article
Times cited : (4)

References (31)
  • 1
    • 0025219013 scopus 로고
    • Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis
    • AMANO A., SHIZUKUISHI S., TAMAGAWA H., IWAKURA K., TSUNASAWA S., TSUNEMTTSU A.: Characterization of superoxide dismutases purified from either anaerobically maintained or aerated Bacteroides gingivalis. J.Bacteriol. 172, 1457-1463 (1990).
    • (1990) J.Bacteriol. , vol.172 , pp. 1457-1463
    • Amano, A.1    Shizukuishi, S.2    Tamagawa, H.3    Iwakura, K.4    Tsunasawa, S.5    Tsunemttsu, A.6
  • 2
    • 0016861525 scopus 로고
    • Superoxide dismutase from a blue-green alga, Plectonema boryanum
    • ASADA K., YOSHIKAWA K., TAKAHASHI M., MAEDA Y., ENMANJI K.: Superoxide dismutase from a blue-green alga, Plectonema boryanum. J.Biol.Chem. 250, 2801-2807 (1975).
    • (1975) J.Biol.Chem. , vol.250 , pp. 2801-2807
    • Asada, K.1    Yoshikawa, K.2    Takahashi, M.3    Maeda, Y.4    Enmanji, K.5
  • 3
    • 0005439348 scopus 로고
    • Superoxide dismutase in ripening fruits
    • BAKER J.E.: Superoxide dismutase in ripening fruits. Plant Physiol. 58, 644-647 (1976).
    • (1976) Plant Physiol. , vol.58 , pp. 644-647
    • Baker, J.E.1
  • 4
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • BEAUCHAMP C., FRIDOVICH I.: Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal.Biochem. 44, 276-287 (1971).
    • (1971) Anal.Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 5
    • 0023124274 scopus 로고
    • Effect of hydrogen peroxide on the iron-containing superoxide dismutase of E. Coli
    • BEYER W.F. Jr., FRIDOVICH I.: Effect of hydrogen peroxide on the iron-containing superoxide dismutase of E. coli. Biochimie 26, 1251-1257 (1987).
    • (1987) Biochimie , vol.26 , pp. 1251-1257
    • Beyer W.F., Jr.1    Fridovich, I.2
  • 7
    • 0028872248 scopus 로고
    • Characterization of 4-superoxide-dismutase genes from a filamentous cyanobacterium
    • CAMPBELL W.S., LAUDENBACH D.E.: Characterization of 4-superoxide-dismutase genes from a filamentous cyanobacterium. J.Bacteriol. 177, 964-972 (1995).
    • (1995) J.Bacteriol. , vol.177 , pp. 964-972
    • Campbell, W.S.1    Laudenbach, D.E.2
  • 8
    • 0028837261 scopus 로고
    • Unusual growth-phase and oxygen-tension regulation of oxidative stress protection enzymes, catalase and superoxide-dismutase in the Phytopathogen xynthomonasoryzae pv. oryzae
    • CHAMNONGPOL S., MONGKOLSUK S., VATTANAVIBOON P., FUANGTHONG M.: Unusual growth-phase and oxygen-tension regulation of oxidative stress protection enzymes, catalase and superoxide-dismutase in the Phytopathogen xynthomonasoryzae pv. oryzae. Appl.Environ.Microbiol. 16, 393-396 (1995).
    • (1995) Appl.Environ.Microbiol. , vol.16 , pp. 393-396
    • Chamnongpol, S.1    Mongkolsuk, S.2    Vattanaviboon, P.3    Fuangthong, M.4
  • 9
    • 0022480378 scopus 로고
    • Superoxide dismutases
    • FRIDOVICH I.: Superoxide dismutases. Adv.Enzymol. 58, 61-97 (1986).
    • (1986) Adv.Enzymol. , vol.58 , pp. 61-97
    • Fridovich, I.1
  • 10
    • 0028119886 scopus 로고
    • Superoxide dismutase level in response to paraquat and high temperature in the cyanobacterium Glœocopsa sp
    • HAMMOUDA O.: Superoxide dismutase level in response to paraquat and high temperature in the cyanobacterium Glœocopsa sp. Biol.Plant. 36, 229-236 (1994).
    • (1994) Biol.Plant. , vol.36 , pp. 229-236
    • Hammouda, O.1
  • 12
    • 0017343504 scopus 로고
    • Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli
    • HASSAN H.M., FRIDOVICH I.: Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli. J.Bacteriol. 129, 1574-1583 (1977).
    • (1977) J.Bacteriol. , vol.129 , pp. 1574-1583
    • Hassan, H.M.1    Fridovich, I.2
  • 14
    • 0011860218 scopus 로고
    • CuZn-SOD from the fern Equisetum arvense and the green alga Spirogyra sp.: Occurrence of chloroplast and cytosol types of enzyme
    • KANEMATSU S., ASADA K.: CuZn-SOD from the fern Equisetum arvense and the green alga Spirogyra sp.: occurrence of chloroplast and cytosol types of enzyme. Plant Cell Physiol. 30, 717-727 (1989).
    • (1989) Plant Cell Physiol. , vol.30 , pp. 717-727
    • Kanematsu, S.1    Asada, K.2
  • 15
    • 0027938939 scopus 로고
    • Importance of anaerobic superoxide dismutase synthesis in facilitating outgrowth of Escherichia coli upon entry into an aerobic habitat
    • KARGALIOGLU V., IMLAY J.A.: Importance of anaerobic superoxide dismutase synthesis in facilitating outgrowth of Escherichia coli upon entry into an aerobic habitat. J.Bacteriol. 176, 7653-7658 (1994).
    • (1994) J.Bacteriol. , vol.176 , pp. 7653-7658
    • Kargalioglu, V.1    Imlay, J.A.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0024653829 scopus 로고
    • Cloning and characterization of an Anacystis nidulans R2 superoxide dismutase gene
    • LAUDENBACH D.E., IRICK C.G., STRAUS N.A.: Cloning and characterization of an Anacystis nidulans R2 superoxide dismutase gene. Mol.Gen.Genet. 216, 455-461 (1989).
    • (1989) Mol.Gen.Genet. , vol.216 , pp. 455-461
    • Laudenbach, D.E.1    Irick, C.G.2    Straus, N.A.3
  • 18
    • 0028913476 scopus 로고
    • Inhibitory effect of oxygen accumulation on the growth of Spirulina platensis
    • MARQUEZ K.J., SASAKI K., NISHIO N., NAGAI S.: Inhibitory effect of oxygen accumulation on the growth of Spirulina platensis. Biotechnol.Lett. 17, 225-228 (1995).
    • (1995) Biotechnol.Lett. , vol.17 , pp. 225-228
    • Marquez, K.J.1    Sasaki, K.2    Nishio, N.3    Nagai, S.4
  • 19
    • 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, 469-474 (1974).
    • (1974) Eur.J.Biochem. , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 20
    • 0028093084 scopus 로고
    • Reactions of hydrogen peroxide with superoxide dismutase from Propionibacterium shermanii - An enzyme which is equally active with iron or manganese are independent of the prosthetic metal
    • MEIER B., SEHN A.R., MICHEL C., SARAN M.: Reactions of hydrogen peroxide with superoxide dismutase from Propionibacterium shermanii - an enzyme which is equally active with iron or manganese are independent of the prosthetic metal. Arch.Biochem.Biophys. 313, 296-303 (1994).
    • (1994) Arch.Biochem.Biophys. , vol.313 , pp. 296-303
    • Meier, B.1    Sehn, A.R.2    Michel, C.3    Saran, M.4
  • 21
    • 0016610311 scopus 로고
    • Purification properties of superoxide dismutase from blue-green algae
    • MISRA H.P., KEEL B.B.: Purification properties of superoxide dismutase from blue-green algae. Biochim.Biophys.Acta 379, 418-425 (1975).
    • (1975) Biochim.Biophys.Acta , vol.379 , pp. 418-425
    • Misra, H.P.1    Keel, B.B.2
  • 22
    • 0017849697 scopus 로고
    • Inhibition of superoxide dismutases by azide
    • MISRA H.P., FRIDOVICH I.: Inhibition of superoxide dismutases by azide. Arch.Biochem.Biophys. 189, 317-322 (1978).
    • (1978) Arch.Biochem.Biophys. , vol.189 , pp. 317-322
    • Misra, H.P.1    Fridovich, I.2
  • 23
    • 0001021482 scopus 로고
    • Chromatography of amino acids sulfonated polystyrene resins
    • MOORE S., SPACKMAN D.H., SIFIN W.H.: Chromatography of amino acids sulfonated polystyrene resins. Anal.Chem. 50, 1105-1190 (1958).
    • (1958) Anal.Chem. , vol.50 , pp. 1105-1190
    • Moore, S.1    Spackman, D.H.2    Sifin, W.H.3
  • 24
    • 0000867260 scopus 로고
    • Intracellular distribution of manganese and ferric superoxide dismutases in blue-green algae
    • OKADA S., KANEMATSU S., ASADA K.: Intracellular distribution of manganese and ferric superoxide dismutases in blue-green algae. FEBS Lett. 103, 106-110 (1979).
    • (1979) FEBS Lett. , vol.103 , pp. 106-110
    • Okada, S.1    Kanematsu, S.2    Asada, K.3
  • 25
    • 0028577345 scopus 로고
    • Regulation of an in vivo metal exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors
    • SEHN A.P., MEIER B.: Regulation of an in vivo metal exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors. Biochem.J. 304, 803-808 (1994).
    • (1994) Biochem.J. , vol.304 , pp. 803-808
    • Sehn, A.P.1    Meier, B.2
  • 26
    • 0021126946 scopus 로고
    • Manganese and iron superoxide dismutase are structural homologs
    • STALLINGS W.C., PATTRIDGE K.A., STRONG R.K., LUDWIG M.L.: Manganese and iron superoxide dismutase are structural homologs. J.Biol.Chem. 259, 10695-10699 (1984).
    • (1984) J.Biol.Chem. , vol.259 , pp. 10695-10699
    • Stallings, W.C.1    Pattridge, K.A.2    Strong, R.K.3    Ludwig, M.L.4
  • 27
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue-green algae (order Chlorococcales)
    • STANIER R.Y., KUNISAWA R., MANDEL M., GOHEN-BAZIRE G.: Purification and properties of unicellular blue-green algae (order Chlorococcales). Bacteriol.Rev. 35, 171-205 (1971).
    • (1971) Bacteriol.rev. , vol.35 , pp. 171-205
    • Stanier, R.Y.1    Kunisawa, R.2    Mandel, M.3    Gohen-Bazire, G.4
  • 28
    • 0025339960 scopus 로고
    • Copper-zinc superoxide dismutase of Caulobacter crescentus: Cloning, sequencing, and mapping of the gene and periplasmic location of tne enzyme
    • STEINMAN H.M., ELY B.: Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of tne enzyme. J.Bacteriol. 6, 2901-2910 (1990).
    • (1990) J.Bacteriol. , vol.6 , pp. 2901-2910
    • Steinman, H.M.1    Ely, B.2
  • 29
    • 0028337813 scopus 로고
    • Expression of superoxide dismutase in Listeria monocytogenes
    • VASCONCELOS J.A.P., DENEER H.G.: Expression of superoxide dismutase in Listeria monocytogenes. Appl.Environ.Microbiol. 60, 2360-2366 (1994).
    • (1994) Appl.Environ.Microbiol. , vol.60 , pp. 2360-2366
    • Vasconcelos, J.A.P.1    Deneer, H.G.2
  • 30
    • 0017289045 scopus 로고
    • Purification, crystallization and properties of iron containing superoxide dismutase from Pseudomonas ovalis
    • YAMAKURA F.: Purification, crystallization and properties of iron containing superoxide dismutase from Pseudomonas ovalis. Biochem.Biophys.Acta 433, 280-294 (1976).
    • (1976) Biochem.Biophys.Acta , vol.433 , pp. 280-294
    • Yamakura, F.1
  • 31
    • 0021774481 scopus 로고
    • Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase
    • YAMAKURA F.: Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase. Biochem.Biophys.Res. Commun. 122, 635-641 (1984).
    • (1984) Biochem.Biophys.Res. Commun. , vol.122 , pp. 635-641
    • Yamakura, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.