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Volumn 5, Issue 1, 2003, Pages 48-54

Diversity of α-halocarboxylic acid dehalogenases in bacteria isolated from a pristine soil after enrichment and selection on the herbicide 2,2-dichloropropionic acid (Dalapon)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; BETAPROTEOBACTERIA; BRADYRHIZOBIUM; BRUCELLA; CULTURE MEDIA; DNA, RIBOSOMAL; HYDROLASES; MOLECULAR SEQUENCE DATA; PHYLOGENY; POACEAE; PROPIONIC ACIDS; PROTEOBACTERIA; RNA, RIBOSOMAL, 16S; SEQUENCE ANALYSIS, DNA; SOIL MICROBIOLOGY; VARIATION (GENETICS);

EID: 0037226865     PISSN: 14622912     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1462-2920.2003.00384.x     Document Type: Article
Times cited : (8)

References (46)
  • 2
    • 0026762899 scopus 로고
    • Cloning and partial sequencing of an operon encoding 2 Pseudomonas putida haloalkanoate dehalogenases of opposite stereospecificity
    • Barth, P.T., Bolton, L., and Thomson, J.C. (1992) Cloning and partial sequencing of an operon encoding 2 Pseudomonas putida haloalkanoate dehalogenases of opposite stereospecificity. J Bacteriol 174: 2612-2619.
    • (1992) J Bacteriol , vol.174 , pp. 2612-2619
    • Barth, P.T.1    Bolton, L.2    Thomson, J.C.3
  • 3
    • 0026503410 scopus 로고
    • Plasmid incidence and linear alkylbenzene sulfonate biodegradation in waste-water and pristine pond ecosystems
    • Breen, A., Jimenez, L., Sayler, G.S., and Federle, T.W. (1992) Plasmid incidence and linear alkylbenzene sulfonate biodegradation in waste-water and pristine pond ecosystems. J Ind Microbiol 9: 37-43.
    • (1992) J Ind Microbiol , vol.9 , pp. 37-43
    • Breen, A.1    Jimenez, L.2    Sayler, G.S.3    Federle, T.W.4
  • 4
    • 0025816929 scopus 로고
    • Survival of alcaligenes-xylosoxidans degrading 2,2-dichloropropionate and horizontal transfer of its halidohydrolase gene in a soil microcosm
    • Brokamp, A., and Schmidt, F.J. (1991) Survival of alcaligenes-xylosoxidans degrading 2,2-dichloropropionate and horizontal transfer of its halidohydrolase gene in a soil microcosm. Curr Microbiol 22: 299-306.
    • (1991) Curr Microbiol , vol.22 , pp. 299-306
    • Brokamp, A.1    Schmidt, F.J.2
  • 5
    • 0030435054 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of a D,L-haloalkanoic acid dehalogenase encoding gene from Alcaligenes xylosoxidans ssp. denitrificans ABIV
    • Brokamp, A., Happe, B., and Schmidt, F.J. (1997a) Cloning and nucleotide sequence of a D,L-haloalkanoic acid dehalogenase encoding gene from Alcaligenes xylosoxidans ssp. denitrificans ABIV. Biodegradation 7: 383-396.
    • (1997) Biodegradation , vol.7 , pp. 383-396
    • Brokamp, A.1    Happe, B.2    Schmidt, F.J.3
  • 6
    • 0031035252 scopus 로고    scopus 로고
    • Homologous plasmids from soil bacteria encoding D,L-halidohydrolases
    • Brokamp, A., Schwarze, R., and Schmidt, F.J. (1997b) Homologous plasmids from soil bacteria encoding D,L-halidohydrolases. Curr Microbiol 34: 97-102.
    • (1997) Curr Microbiol , vol.34 , pp. 97-102
    • Brokamp, A.1    Schwarze, R.2    Schmidt, F.J.3
  • 8
    • 0030026591 scopus 로고    scopus 로고
    • Cloning, sequencing and expression in Eschenchia coli of two Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite stereospecificity
    • Cairns, S.S., Cornish, A., and Cooper, R.A. (1996) Cloning, sequencing and expression in Eschenchia coli of two Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite stereospecificity. Eur J Biochem 235: 744-749.
    • (1996) Eur J Biochem , vol.235 , pp. 744-749
    • Cairns, S.S.1    Cornish, A.2    Cooper, R.A.3
  • 9
    • 0032175395 scopus 로고    scopus 로고
    • Microbial dehalogenases: Enzymes recruited to convert xenobiotic substrates
    • Copley, S.D. (1998) Microbial dehalogenases: enzymes recruited to convert xenobiotic substrates. Curr Opin Chem Biol 2: 613-617.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 613-617
    • Copley, S.D.1
  • 10
    • 0030745978 scopus 로고    scopus 로고
    • Synergistic mineralization of biphenyl by Alcaligenes faecalis type II BPSI-2 and Sphingomonas paucimobilis BPSI-3
    • Davison, A.D., and Veal, D.A. (1997) Synergistic mineralization of biphenyl by Alcaligenes faecalis type II BPSI-2 and Sphingomonas paucimobilis BPSI-3. Lett Appl Microbiol 25: 58-62.
    • (1997) Lett Appl Microbiol , vol.25 , pp. 58-62
    • Davison, A.D.1    Veal, D.A.2
  • 11
    • 0026508240 scopus 로고
    • Mineralization of surfactants in anaerobic sediments of a laundromat wastewater pond
    • Federle, T.W., and Schwab, B.S. (1992) Mineralization of surfactants in anaerobic sediments of a laundromat wastewater pond. Water Res 26: 123-127.
    • (1992) Water Res , vol.26 , pp. 123-127
    • Federle, T.W.1    Schwab, B.S.2
  • 12
    • 0028100163 scopus 로고
    • Bacterial dehalogenases - Biochemistry, genetics, and biotechnological applications
    • Fetzner, S., and Lingens, F. (1994) Bacterial dehalogenases - biochemistry, genetics, and biotechnological applications. Microbiol Rev 58: 641-685.
    • (1994) Microbiol Rev , vol.58 , pp. 641-685
    • Fetzner, S.1    Lingens, F.2
  • 13
    • 0033372395 scopus 로고    scopus 로고
    • A comparison of the ability of forest and agricultural soils to mineralize chlorinated aromatic compounds
    • Fulthorpe, R.R., and Schofield, L.N. (1999) A comparison of the ability of forest and agricultural soils to mineralize chlorinated aromatic compounds. Biodegradation 10: 235-244.
    • (1999) Biodegradation , vol.10 , pp. 235-244
    • Fulthorpe, R.R.1    Schofield, L.N.2
  • 15
    • 0030004561 scopus 로고    scopus 로고
    • Pristine soils mineralize 3-chlorobenzoate and 2,4-dichlorophenoxyacetate via different microbial populations
    • Fulthorpe, R.R., Rhodes, A.N., and Tiedje, J.M. (1996) Pristine soils mineralize 3-chlorobenzoate and 2,4- dichlorophenoxyacetate via different microbial populations. Appl Environ Microbiol 62: 1159-1166.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1159-1166
    • Fulthorpe, R.R.1    Rhodes, A.N.2    Tiedje, J.M.3
  • 16
    • 0031804722 scopus 로고    scopus 로고
    • High levels of endemicity of 3-chlorobenzoate-degrading soil bacteria
    • Fulthorpe, R.R., Rhodes, A.N., and Tiedje, J.M. (1998) High levels of endemicity of 3-chlorobenzoate-degrading soil bacteria. Appl Environ Microbiol 64: 1620-1627.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1620-1627
    • Fulthorpe, R.R.1    Rhodes, A.N.2    Tiedje, J.M.3
  • 17
    • 0030358419 scopus 로고    scopus 로고
    • Naturally occurring organohalogen compounds - A comprehensive survey
    • Gribble, G.W. (1996) Naturally occurring organohalogen compounds - a comprehensive survey. Fortschr Chem Org Naturst 68: 1-423.
    • (1996) Fortschr Chem Org Naturst , vol.68 , pp. 1-423
    • Gribble, G.W.1
  • 18
    • 0026760856 scopus 로고
    • Microbial breakdown of halogenated aromatic pesticides and related-compounds
    • Haggblom, M.M. (1992) Microbial breakdown of halogenated aromatic pesticides and related- compounds. FEMS Microbiol Rev 103: 29-72.
    • (1992) FEMS Microbiol Rev , vol.103 , pp. 29-72
    • Haggblom, M.M.1
  • 19
    • 0032909021 scopus 로고    scopus 로고
    • Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene families
    • Hill, K.E., Marchesi, J.R., and Wefghtman, A.J. (1999) Investigation of two evolutionarily unrelated halocarboxylic acid dehalogenase gene families. J Bacteriol 81: 2535-2547.
    • (1999) J Bacteriol , vol.81 , pp. 2535-2547
    • Hill, K.E.1    Marchesi, J.R.2    Wefghtman, A.J.3
  • 20
    • 0029879609 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL proteins
    • Hisano, T., Hata, Y., Fujii, T., Liu, J.Q., Kurihara, T., Esaki, N., and Soda, K. (1996) Crystallization and preliminary X-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL proteins. Struct Funct Genet 24: 520-522.
    • (1996) Struct Funct Genet , vol.24 , pp. 520-522
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 21
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • Munro, H.N. (ed.). New York: Academic Press
    • Jukes, T.H., and Cantor, C.R. (1969) Evolution of protein molecules. In Mammalian Protein Metabolism. Munro, H.N. (ed.). New York: Academic Press, pp. 21-132.
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 22
    • 0019433725 scopus 로고
    • Rapid procedure for detection and isolation of large and small plasmids
    • Kado, C.I., and Liu, S.T. (1981) Rapid procedure for detection and isolation of large and small plasmids. J Bacteriol 145: 1365-1373.
    • (1981) J Bacteriol , vol.145 , pp. 1365-1373
    • Kado, C.I.1    Liu, S.T.2
  • 23
    • 0031009131 scopus 로고    scopus 로고
    • Pristine environments harbor a new group of oligotrophic 2,4-dichlorophenoxyacetic acid-degrading bacteria
    • Kamagata, Y., Fulthorpe, R.R., Tamura, K., Takami, H., Forney, L.J., and Tiedje, J.M. (1997) Pristine environments harbor a new group of oligotrophic 2,4- dichlorophenoxyacetic acid-degrading bacteria. Appl Environ Microbiol 63: 2266-2272.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2266-2272
    • Kamagata, Y.1    Fulthorpe, R.R.2    Tamura, K.3    Takami, H.4    Forney, L.J.5    Tiedje, J.M.6
  • 24
    • 0000490766 scopus 로고
    • Microbial degradation of 2,2-Dichloropropionic acid in five soils
    • Kaufman, D.D. (1964) Microbial degradation of 2,2-Dichloropropionic acid in five soils. Can J Microbiol 10: 843-852.
    • (1964) Can J Microbiol , vol.10 , pp. 843-852
    • Kaufman, D.D.1
  • 25
    • 0026731450 scopus 로고
    • Lack of homology between 2 haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain-b
    • Kawasaki, H., Tsuda, K., Matsushita, I., and Tonomura, K. (1992) Lack of homology between 2 haloacetate dehalogenase genes encoded on a plasmid from Moraxella sp. strain-b. J Gen Microbiol 138: 1317-1323.
    • (1992) J Gen Microbiol , vol.138 , pp. 1317-1323
    • Kawasaki, H.1    Tsuda, K.2    Matsushita, I.3    Tonomura, K.4
  • 26
    • 0027977735 scopus 로고
    • Cloning and sequence-analysis of a plasmid-encoded 2-haloacid dehalogenase gene from Pseudomonas putida no-109
    • Kawasaki, H., Toyama, T., Maeda, T., Nishino, H., and Tonomura, K. (1994) Cloning and sequence-analysis of a plasmid-encoded 2-haloacid dehalogenase gene from Pseudomonas putida no-109. Biosci Biotechnol Biochem 58: 160-163.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 160-163
    • Kawasaki, H.1    Toyama, T.2    Maeda, T.3    Nishino, H.4    Tonomura, K.5
  • 28
    • 2642677627 scopus 로고    scopus 로고
    • Characteristics and DNA-sequence of a cryptic haloalkanoic acid dehalogenase from Agrobacterium tumefaciens RS5
    • Köhler, R., Brokamp, A., Schwarze, R., Reiting, R.H., and Schmidt, F.J. (1998) Characteristics and DNA-sequence of a cryptic haloalkanoic acid dehalogenase from Agrobacterium tumefaciens RS5. Curr Microbiol 36: 96-101.
    • (1998) Curr Microbiol , vol.36 , pp. 96-101
    • Köhler, R.1    Brokamp, A.2    Schwarze, R.3    Reiting, R.H.4    Schmidt, F.J.5
  • 29
    • 0029006127 scopus 로고
    • Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino-acid-residues
    • Kurihara, T., Liu, J.Q., NardiDei, V., Koshikawa, H., Esaki, N., and Soda, K. (1995) Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino-acid-residues. J Biochem 117: 1317-1322.
    • (1995) J Biochem , vol.117 , pp. 1317-1322
    • Kurihara, T.1    Liu, J.Q.2    NardiDei, V.3    Koshikawa, H.4    Esaki, N.5    Soda, K.6
  • 30
    • 0032510975 scopus 로고    scopus 로고
    • Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism
    • Li, Y.F., Hata, Y., Fujii, T., Hisano, T., Nishihara, M., Kurihara, T., and Esaki, N. (1998) Crystal structures of reaction intermediates of L-2-haloacid dehalogenase and implications for the reaction mechanism. J Biol Chem 273: 15035-15044.
    • (1998) J Biol Chem , vol.273 , pp. 15035-15044
    • Li, Y.F.1    Hata, Y.2    Fujii, T.3    Hisano, T.4    Nishihara, M.5    Kurihara, T.6    Esaki, N.7
  • 31
    • 0031937375 scopus 로고    scopus 로고
    • Design and evaluation of useful bacterium-specific PCR primers that amplify genes coding for bacterial 16S rRNA
    • Marchesi, J.R., Sato, T., Weightman, A.J., Martin, T.A., Fry, J.C., Hiom, S.J., and Wade, W.G. (1998) Design and evaluation of useful bacterium-specific PCR primers that amplify genes coding for bacterial 16S rRNA. Appl Environ Microbiol 64: 795-799.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 795-799
    • Marchesi, J.R.1    Sato, T.2    Weightman, A.J.3    Martin, T.A.4    Fry, J.C.5    Hiom, S.J.6    Wade, W.G.7
  • 32
    • 0026480282 scopus 로고
    • Molecular mechanisms of genetic adaptation to xenobiotic compounds
    • van der Meer, J.R., de Vos, W.M., Harayama, S., and Zehnder, A.J. (1992) Molecular mechanisms of genetic adaptation to xenobiotic compounds. Microbiol Rev 56: 677-694.
    • (1992) Microbiol Rev , vol.56 , pp. 677-694
    • Van Der Meer, J.R.1    De Vos, W.M.2    Harayama, S.3    Zehnder, A.J.4
  • 33
    • 0026555590 scopus 로고
    • Molecular-biology of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4
    • Murdiyatmo, U., Asmara, W., Tsang, J.H., Baines, A.J., Bull, A.T., and Hardman, D.J. (1992) Molecular-biology of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4. Biochem J 284: 87-93.
    • (1992) Biochem J , vol.284 , pp. 87-93
    • Murdiyatmo, U.1    Asmara, W.2    Tsang, J.H.3    Baines, A.J.4    Bull, A.T.5    Hardman, D.J.6
  • 34
    • 0027978786 scopus 로고
    • Comparative-studies of genes encoding thermostable L-2-halo acid dehalogenase from Pseudomonas sp. strain YL, other dehalogenases, and two related hypothetical proteins from Escherichia coli
    • Nardi-Dei, V., Kurihara, T., Okamura, T., Liu, J.Q., Koshikawa, H., Ozaki, H., et al. (1994) Comparative-studies of genes encoding thermostable L-2-halo acid dehalogenase from Pseudomonas sp. strain YL, other dehalogenases, and two related hypothetical proteins from Escherichia coli. Appl Environ Microbiol 60: 3375-3380.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3375-3380
    • Nardi-Dei, V.1    Kurihara, T.2    Okamura, T.3    Liu, J.Q.4    Koshikawa, H.5    Ozaki, H.6
  • 35
    • 0030760868 scopus 로고    scopus 로고
    • Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: Gene cloning and structural comparison with D- and L-2-haloacid dehalogenases
    • Nardi-Dei, V., Kurihara, T., Park, C., Esaki, N., and Soda, K. (1997) Bacterial DL-2-haloacid dehalogenase from Pseudomonas sp. strain 113: gene cloning and structural comparison with D- and L-2-haloacid dehalogenases. J Bacteriol 179: 4232-4238.
    • (1997) J Bacteriol , vol.179 , pp. 4232-4238
    • Nardi-Dei, V.1    Kurihara, T.2    Park, C.3    Esaki, N.4    Soda, K.5
  • 36
    • 0028949105 scopus 로고
    • Adaptation of Xanthobacter autotrophicus GJ10 to bromoacetate due to activation and mobilization of the haloacetate dehalogenase gene by insertion element IS1247
    • van der Ploeg, J.R., Willemsen, M., van Hall, G., and Janssen, D.B. (1995) Adaptation of Xanthobacter autotrophicus GJ10 to bromoacetate due to activation and mobilization of the haloacetate dehalogenase gene by insertion element IS1247. J Bacteriol 177: 1348-1356.
    • (1995) J Bacteriol , vol.177 , pp. 1348-1356
    • Van Der Ploeg, J.R.1    Willemsen, M.2    Van Hall, G.3    Janssen, D.B.4
  • 37
    • 0034029582 scopus 로고    scopus 로고
    • Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-deg radative pathways
    • Poelarends, G.J., Kulakov, L.A., Larkin, M.J., van Hylckama Vlieg, J.E., and Janssen, D.B. (2000) Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-deg radative pathways. J Bacteriol 182: 2191-2199.
    • (2000) J Bacteriol , vol.182 , pp. 2191-2199
    • Poelarends, G.J.1    Kulakov, L.A.2    Larkin, M.J.3    Van Hylckama Vlieg, J.E.4    Janssen, D.B.5
  • 38
    • 0031024099 scopus 로고    scopus 로고
    • Isolation and characterization of dehalogenases from 2,2-dichloropropionate-degrading soil bacteria
    • Schwarze, R., Brokamp, A., and Schmidt, F.J. (1997) Isolation and characterization of dehalogenases from 2,2-dichloropropionate-degrading soil bacteria. Curr Microbiol 34: 103-109.
    • (1997) Curr Microbiol , vol.34 , pp. 103-109
    • Schwarze, R.1    Brokamp, A.2    Schmidt, F.J.3
  • 39
    • 0028291056 scopus 로고
    • Phylogenetic classification of phytopathogenic mollicutes by sequence-analysis of 16S ribosomal DNA
    • Seemuller, E., Schneider, B., Maurer, R., Ahrens, U., Daire, X., Kison, H., et al. (1994) Phylogenetic classification of phytopathogenic mollicutes by sequence-analysis of 16S ribosomal DNA. Int J Syst Bacterio144: 440-446.
    • (1994) Int J Syst Bacterio , vol.144 , pp. 440-446
    • Seemuller, E.1    Schneider, B.2    Maurer, R.3    Ahrens, U.4    Daire, X.5    Kison, H.6
  • 40
    • 0022394254 scopus 로고
    • Dehalogenase genes of Pseudomonas putida PP3 on chromosomally located transposable elements
    • Slater, J.H., Weightman, A.J., and Hall, B.G. (1985) Dehalogenase genes of Pseudomonas putida PP3 on chromosomally located transposable elements. Mol Biol Evol 2: 557-567.
    • (1985) Mol Biol Evol , vol.2 , pp. 557-567
    • Slater, J.H.1    Weightman, A.J.2    Hall, B.G.3
  • 41
    • 0031060628 scopus 로고    scopus 로고
    • Microbial dehalogenation of halogenated alkanoic acids, alcohols and alkanes
    • Slater, J.H., Bull, A.T., and Hardman, D.J. (1997) Microbial dehalogenation of halogenated alkanoic acids, alcohols and alkanes. Adv Microb Physiol 38: 133-176.
    • (1997) Adv Microb Physiol , vol.38 , pp. 133-176
    • Slater, J.H.1    Bull, A.T.2    Hardman, D.J.3
  • 42
    • 0000435582 scopus 로고    scopus 로고
    • Bacterial 2-haloacid dehalogenases: Structures and catalytic properties
    • Soda, K., Kurihara, T., Liu, J.Q., NardiDei, V., Park, C., Miyagi, M., et al. (1996) Bacterial 2-haloacid dehalogenases: structures and catalytic properties. Pure Appl Chem 68' 2097-2103.
    • (1996) Pure Appl Chem , vol.68 , pp. 2097-2103
    • Soda, K.1    Kurihara, T.2    Liu, J.Q.3    NardiDei, V.4    Park, C.5    Miyagi, M.6
  • 43
    • 0031574204 scopus 로고    scopus 로고
    • Haloalkanoate dehalogenase II (DehE) of a Rhizobium sp. - Molecular analysis of the gene and formation of carbon monoxide from trihaloacetate by the enzyme
    • Stringfellow, J.M., Cairns, S.S., Cornish, A., and Cooper, R.A. (1997) Haloalkanoate dehalogenase II (DehE) of a Rhizobium sp. - molecular analysis of the gene and formation of carbon monoxide from trihaloacetate by the enzyme. Eur J Biochem 250: 789-793.
    • (1997) Eur J Biochem , vol.250 , pp. 789-793
    • Stringfellow, J.M.1    Cairns, S.S.2    Cornish, A.3    Cooper, R.A.4
  • 44
    • 0026529669 scopus 로고
    • The dehalogenase gene dehl from Pseudomonas putida PP3 is carried on an unusual mobile genetic element designated deh
    • Thomas, A.W., Slater, J.H., and Weightman, A.J. (1992) The dehalogenase gene dehl from Pseudomonas putida PP3 is carried on an unusual mobile genetic element designated deh. J Bacteriol 174: 1932-1940.
    • (1992) J Bacteriol , vol.174 , pp. 1932-1940
    • Thomas, A.W.1    Slater, J.H.2    Weightman, A.J.3
  • 45
    • 0000560575 scopus 로고
    • A monobromoacetate dehalogenase from Pseudomonas cepacia MBA4
    • Tsang, J.S.H., Sallis, P.J., Bull, A.T., and Hardman, D.J. (1988) A monobromoacetate dehalogenase from Pseudomonas cepacia MBA4. Arch Microbiol 150: 441-446.
    • (1988) Arch Microbiol , vol.150 , pp. 441-446
    • Tsang, J.S.H.1    Sallis, P.J.2    Bull, A.T.3    Hardman, D.J.4
  • 46
    • 0019293583 scopus 로고
    • Selection of Pseudomonas putida strains with elevated dehalogenase activities by continuous culture-growth on chlorinated alkanoic acids
    • Weightman, A.J., and Slater, J.H. (1980) Selection of Pseudomonas putida strains with elevated dehalogenase activities by continuous culture-growth on chlorinated alkanoic acids. J Gen Microbiol 121: 187-193.
    • (1980) J Gen Microbiol , vol.121 , pp. 187-193
    • Weightman, A.J.1    Slater, J.H.2


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