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Volumn 62, Issue 8, 1996, Pages 2940-2946

Identification of an alternative 2,3-dihydroxybiphenyl 1,2-dioxygenase in Rhodococcus sp. strain RHA1 and cloning of the gene

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIHYDROXYBIPHENYL 1,2 DIOXYGENASE; POLYCHLORINATED BIPHENYL; UNCLASSIFIED DRUG;

EID: 0029742571     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.62.8.2940-2946.1996     Document Type: Article
Times cited : (50)

References (46)
  • 1
    • 0015540224 scopus 로고
    • Degradation of chlorinated biphenyls by two species of Achromobacter
    • Ahmad, M., and D. B. Focht. 1973. Degradation of chlorinated biphenyls by two species of Achromobacter. Can. J. Microbiol. 19:47-52.
    • (1973) Can. J. Microbiol. , vol.19 , pp. 47-52
    • Ahmad, M.1    Focht, D.B.2
  • 2
    • 0028122061 scopus 로고
    • Formation of chlorocatecho! mêla cleavage products by a pseudomonad during metabolism of monochlorobiphenyls
    • Arensdorf, J. J., and D. D. Focht. 1994. Formation of chlorocatecho! mêla cleavage products by a pseudomonad during metabolism of monochlorobiphenyls. Appl. Environ. Microbiol. 60:2884-2889.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2884-2889
    • Arensdorf, J.J.1    Focht, D.D.2
  • 3
    • 0028276797 scopus 로고
    • Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rliodococcus globenilus P6
    • Asturias, J. A., L. D. Eltis, M. Prucha, and K. N. Timmis. 1994. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rliodococcus globenilus P6. J. Biol. Chem. 269:7807-7815.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7807-7815
    • Asturias, J.A.1    Eltis, L.D.2    Prucha, M.3    Timmis, K.N.4
  • 4
    • 0027250341 scopus 로고
    • Three different 2,3-dihydroxybiphenyl-l,2-dioxygcnase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rliodococcus globerulus P6
    • Asturias, J. A., and K. N. Timmis. 1993. Three different 2,3-dihydroxybiphenyl-l,2-dioxygcnase genes in the gram-positive polychlorobiphenyl-degrading bacterium Rliodococcus globerulus P6. J. Bacteriol. 175:4631-4540.
    • (1993) J. Bacteriol. , vol.175 , pp. 4631-14540
    • Asturias, J.A.1    Timmis, K.N.2
  • 6
    • 0023190735 scopus 로고
    • Evidence for novel mechanisms of polychlorinated biphenyl metabolism in Alcaligenes eulrophus H850
    • Bedard, D. L., M. L. Haberl, R. J. May, and M. J. Brennan. 1987. Evidence for novel mechanisms of polychlorinated biphenyl metabolism in Alcaligenes eulrophus H850. Appl. Environ. Microbiol. 53:1103-1112.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 1103-1112
    • Bedard, D.L.1    Haberl, M.L.2    May, R.J.3    Brennan, M.J.4
  • 7
    • 0022621961 scopus 로고
    • Rapid assay for screening and characterizing microorganisms for the ability to degrade polychlorinated biphenyls
    • Bedard, D. L., R. Unterman, L. H. Bopp, M. J. Brennan, M. L. Haberl, and C. Johnson. 1986. Rapid assay for screening and characterizing microorganisms for the ability to degrade polychlorinated biphenyls. Appl. Environ. Microbiol. 51:761-768.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 761-768
    • Bedard, D.L.1    Unterman, R.2    Bopp, L.H.3    Brennan, M.J.4    Haberl, M.L.5    Johnson, C.6
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0028324162 scopus 로고
    • The catechol 2,3-dioxygenase gene of Rliodococcus rhodochrous CTM: Nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine
    • Candidas, S., K.-H. van Pee, and F. Lingens. 1994. The catechol 2,3-dioxygenase gene of Rliodococcus rhodochrous CTM: nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine. Microbiology (Reading) 140:321-330.
    • (1994) Microbiology (Reading) , vol.140 , pp. 321-330
    • Candidas, S.1    Van Pee, K.-H.2    Lingens, F.3
  • 12
    • 0027509616 scopus 로고
    • Purification and crystallization of 2,3-dihydroxybiphenyl-l,2-dioxygenase
    • Eltis, L. D., B. Hofmann, H.-J. Hecht, H. Lunsdorf, and K. N. Timmis. 1993. Purification and crystallization of 2,3-dihydroxybiphenyl-l,2-dioxygenase. J. Biol. Chem. 268:2727-2732.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2727-2732
    • Eltis, L.D.1    Hofmann, B.2    Hecht, H.-J.3    Lunsdorf, H.4    Timmis, K.N.5
  • 13
    • 0026766452 scopus 로고
    • Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400
    • Erickson, B. D., and F. J. Mondello. 1992. Nucleotide sequencing and transcriptional mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400. J. Bacteriol. 174:2903-2912.
    • (1992) J. Bacteriol. , vol.174 , pp. 2903-2912
    • Erickson, B.D.1    Mondello, F.J.2
  • 14
    • 0027368828 scopus 로고
    • Enhanced biodégradation of polychlorinated biphenyls after site-directed mutagenesis of a biphenyl dioxygenase gene
    • Erickson, B. D., and F. J. Mondello. 1993. Enhanced biodégradation of polychlorinated biphenyls after site-directed mutagenesis of a biphenyl dioxygenase gene. Appl. Environ. Microbiol. 59:3858-3862.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3858-3862
    • Erickson, B.D.1    Mondello, F.J.2
  • 15
    • 0023114367 scopus 로고
    • Purification and properties of 2,3dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene
    • Furukawa, K-, and N. Arimura. 1987. Purification and properties of 2,3dihydroxybiphenyl dioxygenase from polychlorinated biphenyl-degrading Pseudomonas pseudoalcaligenes and Pseudomonas aeruginosa carrying the cloned bphC gene. J. Bacteriol. 169:924-927.
    • (1987) J. Bacteriol. , vol.169 , pp. 924-927
    • Furukawa, K.1    Arimura, N.2
  • 16
    • 0023120324 scopus 로고
    • Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes
    • Furukawa, K., N. Arimura, and T. Miyazaki. 1989. Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes. J. Bacteriol. 169:427-429.
    • (1989) J. Bacteriol. , vol.169 , pp. 427-429
    • Furukawa, K.1    Arimura, N.2    Miyazaki, T.3
  • 17
    • 0027223958 scopus 로고
    • Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bpli operon) and toluene (tod operon)
    • Furukawa, K., J. Hirose, A. Suyama, T. Zaiki, and S. Hayashida. 1993. Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bpli operon) and toluene (tod operon). J. Bacteriol. 175:52245232.
    • (1993) J. Bacteriol. , vol.175 , pp. 52245232
    • Furukawa, K.1    Hirose, J.2    Suyama, A.3    Zaiki, T.4    Hayashida, S.5
  • 18
    • 0022617112 scopus 로고
    • Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes. 3
    • Furukawa, K., and T. Miyazaki. 1986. Cloning of a gene cluster encoding biphenyl and chlorobiphenyl degradation in Pseudomonas pseudoalcaligenes. 3. Bacteriol. 166:392-398.
    • (1986) Bacteriol. , vol.166 , pp. 392-398
    • Furukawa, K.1    Miyazaki, T.2
  • 19
    • 0018306487 scopus 로고
    • Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls
    • Furukawa, K., N. Tomizuka, and A. Kamibayashi. 1979. Effect of chlorine substitution on the bacterial metabolism of various polychlorinated biphenyls. Appl. Environ. Microbiol. 38:301-310.
    • (1979) Appl. Environ. Microbiol. , vol.38 , pp. 301-310
    • Furukawa, K.1    Tomizuka, N.2    Kamibayashi, A.3
  • 20
    • 0023178007 scopus 로고
    • Nucleotide sequence and expression of gene nalM of plasmid NAH7 and homology with gene xylE of TOL pWWO
    • Ghosal, D., I.-S. You, and I. C. Gunsalus. 1987. Nucleotide sequence and expression of gene nalM of plasmid NAH7 and homology with gene xylE of TOL pWWO. Gene 55:19-25.
    • (1987) Gene , vol.55 , pp. 19-25
    • Ghosal, D.1    You, I.-S.2    Gunsalus, I.C.3
  • 21
    • 0021112458 scopus 로고
    • An improved strategy for rapid direct sequencing of both strands of long DMA molecules cloned in a plasmid
    • Guo, L. H., R. C. Yang, and R. Wu. 1983. An improved strategy for rapid direct sequencing of both strands of long DMA molecules cloned in a plasmid. Nucleic Acids Res. 11:5521-5540.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 5521-5540
    • Guo, L.H.1    Yang, R.C.2    Wu, R.3
  • 22
    • 0027442082 scopus 로고
    • Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- And dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1
    • Happe, B., L. D. Eltis, H. Poth, R. Hedderich, and K. N. Timmis. 1993. ' Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1. J. Bacteriol. 175:7313 7320: - '
    • (1993) J. Bacteriol. , vol.175 , pp. 7313-7320
    • Happe, B.1    Eltis, L.D.2    Poth, H.3    Hedderich, R.4    Timmis, K.N.5
  • 23
    • 0024451702 scopus 로고
    • Comparison of the nucleotide sequences of the mera-cleavage pathway genes of TOL plasmid pWWO from Pseudo-monas pittida with other m#a-cleavage genes suggests that both single and multiple nucleotide substitutions contribute to enzyme evolution
    • Harayama, S., and M. Rekik. 1989. Comparison of the nucleotide sequences of the mera-cleavage pathway genes of TOL plasmid pWWO from Pseudo-monas pittida with other m#a-cleavage genes suggests that both single and multiple nucleotide substitutions contribute to enzyme evolution. J. Biol. Chem. 264:15328-15332.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15328-15332
    • Harayama, S.1    Rekik, M.2
  • 24
    • 33847473562 scopus 로고    scopus 로고
    • Gene cloning and characterization of 2,3-dihydroxybiphenyl dioxygenase from the PCBdegrading gram-positive bacterium Rliodococcus sp
    • Hatta, T., K. Kimbara, M. Fukuda, H. Kiyohara, and K. Yano. Gene cloning and characterization of 2,3-dihydroxybiphenyl dioxygenase from the PCBdegrading gram-positive bacterium Rliodococcus sp. RHA1. Submitted for publication.
    • RHA1. Submitted for Publication.
    • Hatta, T.1    Kimbara, K.2    Fukuda, M.3    Kiyohara, H.4    Yano, K.5
  • 25
    • 0025020696 scopus 로고
    • Pseudomonas putida KF715 bpliABCD opcron encoding biphenyl and polychlorinated biphenyl degradation: Cloning, analysis, and expression in soil bacteria
    • Hayase, N., K. Taira, and K. Furukawa. 1990. Pseudomonas putida KF715 bpliABCD opcron encoding biphenyl and polychlorinated biphenyl degradation: cloning, analysis, and expression in soil bacteria. J. Bacteriol. 172:11601164.
    • (1990) J. Bacteriol. , vol.172 , pp. 11601164
    • Hayase, N.1    Taira, K.2    Furukawa, K.3
  • 26
    • 0028215858 scopus 로고
    • Construction of hybrid biphenyl and toluene genes for functional analysis of aromatic ring dioxygenases
    • Ilirosc, J., A. Suyama, S. Hayashida, and K. Furukawa. 1994. Construction of hybrid biphenyl and toluene genes for functional analysis of aromatic ring dioxygenases. Gene 138:27-33.
    • (1994) Gene , vol.138 , pp. 27-33
    • Ilirosc, J.1    Suyama, A.2    Hayashida, S.3    Furukawa, K.4
  • 27
    • 0025165613 scopus 로고
    • Nucleotide sequence of the metapyrocatechase II (catechol 2,3-oxygenase II) gene mpcll from Alcaligenes eulrophus JMP 222
    • Kabisch, M, and P. Fortnagel. 1990. Nucleotide sequence of the metapyrocatechase II (catechol 2,3-oxygenase II) gene mpcll from Alcaligenes eulrophus JMP 222. Nucleic Acids Res. 18:5543.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5543
    • Kabisch, M.1    Fortnagel, P.2
  • 28
    • 0019457548 scopus 로고
    • Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol
    • Klecka, G. M, and D. T. Gibson. 1981. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol. Appl. Environ. Microbiol. 41:1159-1165.
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 1159-1165
    • Klecka, G.M.1    Gibson, D.T.2
  • 29
    • 0023693287 scopus 로고
    • Cometabolism of polychlorinated biphenyls: Enhanced transformation of Aroclor 1254 by growing bacterial cells
    • Kohler, H.-P. E., D. Kohler-Staub, and D. D. Focht. 1988. Cometabolism of polychlorinated biphenyls: enhanced transformation of Aroclor 1254 by growing bacterial cells. Appl. Environ. Microbiol. 54:1940-1945.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1940-1945
    • Kohler, H.-P.E.1    Kohler-Staub, D.2    Focht, D.D.3
  • 30
    • 0024562664 scopus 로고
    • Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102
    • Kimbara, K., T. Hashimoto, M. Fukuda, T. Koana, M. Takagi, M. Oishi, and K. Yano. 1989. Cloning and sequencing of two tandem genes involved in degradation of 2,3-dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading soil bacterium Pseudomonas sp. strain KKS102. J. Bacteriol. 171:2740-2747.
    • (1989) J. Bacteriol. , vol.171 , pp. 2740-2747
    • Kimbara, K.1    Hashimoto, T.2    Fukuda, M.3    Koana, T.4    Takagi, M.5    Oishi, M.6    Yano, K.7
  • 31
    • 0025773011 scopus 로고
    • Purification and characterization of a l,2-dihydroxynaphtha!ene dioxygenase from a bacterium that degrades naphthalenesulfonic acids
    • Kuhm, A. E., A. Stolz, K.-L. Ngai, and H.-J. Knackmuss. 1991. Purification and characterization of a l,2-dihydroxynaphtha!ene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J. Bacteriol. 173:3795-3802.
    • (1991) J. Bacteriol. , vol.173 , pp. 3795-3802
    • Kuhm, A.E.1    Stolz, A.2    Ngai, K.-L.3    Knackmuss, H.-J.4
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0028797047 scopus 로고
    • Multiple genes encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase in the gram-positive polychlorinated biphenyl-degrading bacterium Rliodococcus erylhropolis TA421, isolated from a termite ecosystem
    • Maeda, M., S.-Y. Chung, E. Song, and T. Kudo. 1995. Multiple genes encoding 2,3-dihydroxybiphenyl 1,2-dioxygenase in the gram-positive polychlorinated biphenyl-degrading bacterium Rliodococcus erylhropolis TA421, isolated from a termite ecosystem. Appl. Environ. Microbiol. 61:549-555.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 549-555
    • Maeda, M.1    Chung, S.-Y.2    Song, E.3    Kudo, T.4
  • 34
    • 0029059059 scopus 로고
    • Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl dégrader Rliodococcus sp. strain RHA1
    • Masai, E., A. Yamada, J. M. Healy, T. Hatla, K. Kimbara, M. Fukuda, and K. Yano. 1995. Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl dégrader Rliodococcus sp. strain RHA1. Appl. Environ. Microbiol. 61:2079-2085.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2079-2085
    • Masai, E.1    Yamada, A.2    Healy, J.M.3    Hatla, T.4    Kimbara, K.5    Fukuda, M.6    Yano, K.7
  • 35
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonasputida mt-2
    • Nakai, C., H. Kagamiyama, M. Nozaki, T. Nakazawa, S. Inouye, Y. Ebina, and A. Nakazawa. 1983. Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid of Pseudomonasputida mt-2. J. Biol. Chem. 258:2923-2928.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Ebina, Y.6    Nakazawa, A.7
  • 36
    • 0017342054 scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Porzio, M. A., and A. M. Pearson. 1977. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta 490:27-34.
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 37
    • 0023667753 scopus 로고
    • Redesigning metabolic routes: Manipulation of TOL plasmid pathway for catabolism of alkylbenzoates
    • Ramos, J. L., A. Wasserfallen, K. Rose, and K. N. Timmis. 1987. Redesigning metabolic routes: manipulation of TOL plasmid pathway for catabolism of alkylbenzoates. Science 235:593-596.
    • (1987) Science , vol.235 , pp. 593-596
    • Ramos, J.L.1    Wasserfallen, A.2    Rose, K.3    Timmis, K.N.4
  • 40
    • 0029128756 scopus 로고
    • A novel transformation of polychlorinated biphenyls by Rliodococcus sp. strain RHA1
    • Seto, M., K. Kimbara, M. Shimura, T. Hatta, M. Fukuda, and K. Yano. 1995. A novel transformation of polychlorinated biphenyls by Rliodococcus sp. strain RHA1. Appl. Environ. Microbiol. 61:3353-3358.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3353-3358
    • Seto, M.1    Kimbara, K.2    Shimura, M.3    Hatta, T.4    Fukuda, M.5    Yano, K.6
  • 41
    • 0028837539 scopus 로고
    • Multiple polychlorinated biphenyl transformation systems in the grampositive bacterium Rliodococcus sp. strain RHA1
    • Seto, M., E. Masai, M. Ida, T. Hatta, K. Kimbara, M. Fukuda, and K. Yano. 1995. Multiple polychlorinated biphenyl transformation systems in the grampositive bacterium Rliodococcus sp. strain RHA1. Appl. Environ. Microbiol. 61:4510-4513.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4510-4513
    • Seto, M.1    Masai, E.2    Ida, M.3    Hatta, T.4    Kimbara, K.5    Fukuda, M.6    Yano, K.7
  • 42
    • 0026567783 scopus 로고
    • Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600
    • Shingler, V., J. Powlowski, and U. Marklund. 1992. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174:711-724.
    • (1992) J. Bacteriol. , vol.174 , pp. 711-724
    • Shingler, V.1    Powlowski, J.2    Marklund, U.3
  • 43
    • 0026557457 scopus 로고
    • Effects of chlorobenzoate transformation on the Pseudomonas testosteroni biphenyl and chlorobiphenyl degradation pathway
    • Sondossi, M., M. Sylvestre, and D. Ahmad. 1992. Effects of chlorobenzoate transformation on the Pseudomonas testosteroni biphenyl and chlorobiphenyl degradation pathway. Appl. Environ. Microbiol. 58:485-495.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 485-495
    • Sondossi, M.1    Sylvestre, M.2    Ahmad, D.3
  • 44
    • 0024300820 scopus 로고
    • Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Ql
    • Taira, K., N. Hayase, N. Arimura, S. Yamashita, T. Miyazaki, and K. Furukavra. 1989. Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Ql. Biochemistry 27:3990-3996.
    • (1989) Biochemistry , vol.27 , pp. 3990-3996
    • Taira, K.1    Hayase, N.2    Arimura, N.3    Yamashita, S.4    Miyazaki, T.5    Furukavra, K.6
  • 45
    • 0000822783 scopus 로고
    • Preparative and analytical purification of DNA from agarose
    • Vogelstein, B., and D. Gillespie. 1979. Preparative and analytical purification of DNA from agarose. Proc. Natl. Acad. Sei. USA 76:615-619.
    • (1979) Proc. Natl. Acad. Sei. USA , vol.76 , pp. 615-619
    • Vogelstein, B.1    Gillespie, D.2
  • 46
    • 0024427069 scopus 로고
    • Toluene degradation by Pseudomonas putida Fl: Nucleotide sequence of the toddC2BADE genes and their expression in Escherichia coli
    • Zylstra, G. J., and D. T. Gibson. 1989. Toluene degradation by Pseudomonas putida Fl: nucleotide sequence of the toddC2BADE genes and their expression in Escherichia coli. J. Biol. Chem. 264:14940-14946.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14940-14946
    • Zylstra, G.J.1    Gibson, D.T.2


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