메뉴 건너뛰기




Volumn 47, Issue 3, 2002, Pages 235-240

Oxidative stress-induced expression of catalases in Comamonas terrigena

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); COMAMONAS; COMAMONAS TERRIGENA; FELIS CATUS; NEGIBACTERIA;

EID: 0041370229     PISSN: 00155632     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02817644     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dve binding
    • BRADFORD M.M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dve binding. Anal.Biochem. 72, 248-254 (1976).
    • (1976) Anal.Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0023279475 scopus 로고
    • The use of N,N,N′,N′-tetramethylphenylenediamine to detect peroxidase activity on polyacrylamide electrophoresis gels
    • BUTLER M.J., LACHANCE M.; The use of N,N,N′,N′-tetramethylphenylenediamine to detect peroxidase activity on polyacrylamide electrophoresis gels. Anal. Biochem. 162, 443-445 (1987).
    • (1987) Anal. Biochem. , vol.162 , pp. 443-445
    • Butler, M.J.1    Lachance, M.2
  • 4
    • 0043262765 scopus 로고    scopus 로고
    • Effect of starvation and chloramphenicol on acceleration of bacterial dihexyl sulfosuccinate biotransformation
    • CHMELÁROVÁ Z., ZÁVADSKÁ I., HÚSKA J., TÓTH D.: Effect of starvation and chloramphenicol on acceleration of bacterial dihexyl sulfosuccinate biotransformation. Folia Microbiol. 45, 493-495 (2000b).
    • (2000) Folia Microbiol. , vol.45 , pp. 493-495
    • Chmelárová, Z.1    Závadská, I.2    Húska, J.3    Tóth, D.4
  • 5
    • 0030589073 scopus 로고    scopus 로고
    • Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE
    • ENGELMANN S., HECKER M.: Impaired oxidative stress resistance of Bacillus subtilis sigB mutants and the role of katA and katE. FEMS
    • (1996) FEMS Microbiol. Lett. , vol.145 , pp. 63-69
    • Engelmann, S.1    Hecker, M.2
  • 6
    • 2642642931 scopus 로고    scopus 로고
    • Cloning, characterization, and targeted disruption of cpcat1, coding for an in planta-secreted catalase of Claviveps purpurea
    • GARRE V., MULLER U., TUDZYNSKI P.: Cloning, characterization, and targeted disruption of cpcat1, coding for an in planta-secreted catalase of Claviveps purpurea. Mol. Plant-Microbe Interact. 11, 772-783 (1998).
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 772-783
    • Garre, V.1    Muller, U.2    Tudzynski, P.3
  • 7
    • 0043249100 scopus 로고    scopus 로고
    • Alcohol dehydrogenase involved in the microbial degradation of dioctyl sulfosuccinate
    • GODOCÍKOVÁ J., POLEK B., FERIANC P., TÓTH D.: Alcohol dehydrogenase involved in the microbial degradation of dioctyl sulfosuccinate. Chem. Listy 90, 759 (1996).
    • (1996) Chem. Listy , vol.90 , pp. 759
    • Godocíková, J.1    Polek, B.2    Ferianc, P.3    Tóth, D.4
  • 9
    • 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
  • 10
    • 0029946166 scopus 로고    scopus 로고
    • Anomalous phylogenies based on bacterial catalase gene sequences
    • MAYFIELD J.E., DUVALL, M.R.: Anomalous phylogenies based on bacterial catalase gene sequences. J.Mol.Evol. 42, 469-471 (1996).
    • (1996) J.Mol.Evol. , vol.42 , pp. 469-471
    • Mayfield, J.E.1    Duvall, M.R.2
  • 12
    • 0020422181 scopus 로고
    • Catalase from Comamonas compransoris
    • NIES D., SCHLEGEL H.G.: Catalase from Comamonas compransoris. J.Gen.Appl.Microbiol. 28, 311-319 (1982).
    • (1982) J.Gen.Appl.Microbiol. , vol.28 , pp. 311-319
    • Nies, D.1    Schlegel, H.G.2
  • 13
    • 0031301650 scopus 로고    scopus 로고
    • Enrichment, isolation and characterization of dialkyl sulfosuccinate degrading bacteria Comamonas terrigena N3H and Comamonas terrigena NIC
    • PROKŠOVÁ M., AUGUSTÍN J., VRBANOVÁ A.: Enrichment, isolation and characterization of dialkyl sulfosuccinate degrading bacteria Comamonas terrigena N3H and Comamonas terrigena NIC. Folia Microbiol. 42, 635-639 (1997).
    • (1997) Folia Microbiol. , vol.42 , pp. 635-639
    • Prokšová, M.1    Augustín, J.2    Vrbanová, A.3
  • 14
    • 0029848194 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobe Bacteroides fragilis: A role for catalase in protection against hydrogen peroxide
    • ROCHA E.R., SELBY T., COLEMAN J.P., SMITH C.J.: Oxidative stress response in an anaerobe Bacteroides fragilis: a role for catalase in protection against hydrogen peroxide. J.Bacteriol. 178, 6895-6903 (1996).
    • (1996) J.Bacteriol. , vol.178 , pp. 6895-6903
    • Rocha, E.R.1    Selby, T.2    Coleman, J.P.3    Smith, C.J.4
  • 15
    • 0016170267 scopus 로고
    • Microbial assimilation of methanol and function of catalase in Candida boidinii
    • ROGGENKAMP R., SAHM H., WAGNER F.: Microbial assimilation of methanol and function of catalase in Candida boidinii. FEBS Lett. 41, 283-286 (1974).
    • (1974) FEBS Lett. , vol.41 , pp. 283-286
    • Roggenkamp, R.1    Sahm, H.2    Wagner, F.3
  • 16
    • 0033290056 scopus 로고    scopus 로고
    • Oxidative stress in microorganisms - I. Microbial vs. higher cells - Damage and defenses in relation to cell aging and death
    • SIGLER K., CHALOUPKA J., BROZMANOVÁ J., STADLER N., HÖFER M.: Oxidative stress in microorganisms - I. Microbial vs. higher cells - damage and defenses in relation to cell aging and death. Folia Microbiol. 44, 587-624 (1999).
    • (1999) Folia Microbiol. , vol.44 , pp. 587-624
    • Sigler, K.1    Chaloupka, J.2    Brozmanová, J.3    Stadler, N.4    Höfer, M.5
  • 17
    • 0019295517 scopus 로고
    • The peroxidatic and catalatic activity of catalase in normal and acatalasemic mouse liver
    • SRIVASTAVA S.K., ANSARI N.H.; The peroxidatic and catalatic activity of catalase in normal and acatalasemic mouse liver. Biochim. Biophys.Acta 633, 317-322 (1980).
    • (1980) Biochim. Biophys.Acta , vol.633 , pp. 317-322
    • Srivastava, S.K.1    Ansari, N.H.2
  • 18
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • STOHS S. J., BAGCHI D.: Oxidative mechanisms in the toxicity of metal ions. Free Radic.Biol.Med. 18, 321-336 (1995).
    • (1995) Free Radic.Biol.Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 19
    • 0031840087 scopus 로고    scopus 로고
    • Purification and characteriZation of a catalase from the nonsulplrur phototropic bacterium Rhodobacter sphaeroides ATH 2.4.1 and its role in the oxidative stress response
    • TERZENBACH D.P., BLAUT M.: Purification and characteriZation of a catalase from the nonsulplrur phototropic bacterium Rhodobacter sphaeroides ATH 2.4.1 and its role in the oxidative stress response. Arch.Microbiol. 169, 503-508 (1998).
    • (1998) Arch.Microbiol. , vol.169 , pp. 503-508
    • Terzenbach, D.P.1    Blaut, M.2
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • TOWBIN H., STAEHELIN T., GORDON J.: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc.Nat.Acad.Sci. USA 76, 4350-4354 (1979).
    • (1979) Proc.Nat.Acad.Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 21
    • 0030840083 scopus 로고    scopus 로고
    • RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains
    • VISICK J.E., CLARKE S.: RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains. J.Bacteriol. 179, 4158-4163 (1997).
    • (1997) J.Bacteriol. , vol.179 , pp. 4158-4163
    • Visick, J.E.1    Clarke, S.2
  • 22
    • 0015152970 scopus 로고
    • An improved procedure using ferricyanide for detecting catalase isozymes
    • WOODBURY W., SPENCER A.K., STAHMAN M.A.: An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem. 44, 301-305 (1971).
    • (1971) Anal. Biochem. , vol.44 , pp. 301-305
    • Woodbury, W.1    Spencer, A.K.2    Stahman, M.A.3
  • 23
    • 0345777642 scopus 로고    scopus 로고
    • Spectroscopic and enzymatic features of yeast peroxisomal catalase
    • ZÁMOCKÝ M.: Spectroscopic and enzymatic features of yeast peroxisomal catalase. Chem. Listy 92, 875-882 (1998).
    • (1998) Chem. Listy , vol.92 , pp. 875-882
    • Zámocký, M.1
  • 24
    • 0038360689 scopus 로고    scopus 로고
    • Understanding the structure and function of catalases: Clues from molecular evolution and in vitro mutagenesis
    • ZÁMOCKÝ M.; KOLLER F.: Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Progr.Biophys.Mol.Biol. 72, 19-66 (1999).
    • (1999) Progr.Biophys.Mol.biol. , vol.72 , pp. 19-66
    • Zámocký, M.1    Koller, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.