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Volumn 144, Issue 6, 1998, Pages 1659-1667

The NADH-dependent glutamate dehydrogenase enzyme of Bacteroides fragilis Bf1 is induced by peptides in the growth medium

Author keywords

Bacteroides fragilis; Glutamate dehydrogenase; Nitrogen metabolism

Indexed keywords

BACTERIAL ENZYME; GLUTAMATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0031779512     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-144-6-1659     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0022402080 scopus 로고
    • Isolation and physiological characterisation of mitomycin C-sensitive/UV-sensitive mutants in Bacteroides fragilis
    • Abratt, V. R., Jones, D. T. & Woods, D. R. (1985). Isolation and physiological characterisation of mitomycin C-sensitive/UV-sensitive mutants in Bacteroides fragilis. J Gen Microbiol 131, 2479-2483.
    • (1985) J Gen Microbiol , vol.131 , pp. 2479-2483
    • Abratt, V.R.1    Jones, D.T.2    Woods, D.R.3
  • 2
    • 0027522743 scopus 로고
    • A reporter gene vector to investigate the regulation of glutamine synthetase in Bacteroides fragilis Bf1
    • Abratt, V. R., Zappe, H. & Woods, D. R. (1993). A reporter gene vector to investigate the regulation of glutamine synthetase in Bacteroides fragilis Bf1. J Gen Microbiol 139, 59-65.
    • (1993) J Gen Microbiol , vol.139 , pp. 59-65
    • Abratt, V.R.1    Zappe, H.2    Woods, D.R.3
  • 3
    • 0019888537 scopus 로고
    • Evidence for two functional gal promoters in intact Escherichia coli cells
    • Aiba, H., Adhya, S. & de Crombrugghe, B. (1981). Evidence for two functional gal promoters in intact Escherichia coli cells. J Biol Chem 256, 11905-11910.
    • (1981) J Biol Chem , vol.256 , pp. 11905-11910
    • Aiba, H.1    Adhya, S.2    De Crombrugghe, B.3
  • 4
    • 0030448724 scopus 로고    scopus 로고
    • The NAD(P)H-utilising glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by transacting gene(s) positioned downstream of gdhA
    • Baggio, L. &. Morrison, M. (1996). The NAD(P)H-utilising glutamate dehydrogenase of Bacteroides thetaiotaomicron belongs to enzyme family I, and its activity is affected by transacting gene(s) positioned downstream of gdhA. J Bacteriol 178, 7212-7220.
    • (1996) J Bacteriol , vol.178 , pp. 7212-7220
    • Baggio, L.1    Morrison, M.2
  • 5
    • 0025790495 scopus 로고
    • The gene for a halophilic glutamate dehydrogenase: Sequence, transcriptional analysis and phylogenetic implications
    • Benachenhou, N. & Baldacci, G. (1991). The gene for a halophilic glutamate dehydrogenase: sequence, transcriptional analysis and phylogenetic implications. Mol Gen Genet 230, 345-352.
    • (1991) Mol Gen Genet , vol.230 , pp. 345-352
    • Benachenhou, N.1    Baldacci, G.2
  • 6
    • 0027416155 scopus 로고
    • Evolution of glutamate dehydrogenase genes: Evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life
    • Benachenhou-Lahfa, N., Forterre, P. & Labedan, B. (1993). Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. J Mol Evol 36, 335-346.
    • (1993) J Mol Evol , vol.36 , pp. 335-346
    • Benachenhou-Lahfa, N.1    Forterre, P.2    Labedan, B.3
  • 7
    • 0026756915 scopus 로고
    • GltF, a member of the gltBDF operon of Escherichia coli, is involved in nitrogen-regulated gene expression
    • Castano, I., Flores, N., Valle, F., Covarrubias, A. A. & Bolivar, F. (1992). gltF, a member of the gltBDF operon of Escherichia coli, is involved in nitrogen-regulated gene expression. Mol Microbiol 6, 2733-2741.
    • (1992) Mol Microbiol , vol.6 , pp. 2733-2741
    • Castano, I.1    Flores, N.2    Valle, F.3    Covarrubias, A.A.4    Bolivar, F.5
  • 8
    • 0029589429 scopus 로고
    • Purification and characterisation of a fibrinogen-degrading protease in Bacteroides fragilis strain YCH46
    • Chen, Y., Kinouchi, T., Kataoka, K., Akimoto, S. & Ohnishi, Y. (1995). Purification and characterisation of a fibrinogen-degrading protease in Bacteroides fragilis strain YCH46. Microb Immunol 39, 967-977.
    • (1995) Microb Immunol , vol.39 , pp. 967-977
    • Chen, Y.1    Kinouchi, T.2    Kataoka, K.3    Akimoto, S.4    Ohnishi, Y.5
  • 9
    • 0026289417 scopus 로고
    • Identification of the major surface protein antigens of Porphyromonas gingivalis using IgG antibody reactivity of periodontal case-control serum
    • Curtis, M. A., Slaney, J. M., Carman, R. J. & Johnson, N. W. (1991). Identification of the major surface protein antigens of Porphyromonas gingivalis using IgG antibody reactivity of periodontal case-control serum. Oral Microbiol Immunol 6, 321-326.
    • (1991) Oral Microbiol Immunol , vol.6 , pp. 321-326
    • Curtis, M.A.1    Slaney, J.M.2    Carman, R.J.3    Johnson, N.W.4
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. & Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12, 387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0026462830 scopus 로고
    • Purification and properties of NADP-dependent glutamate dehydrogenase from Ruminococcus flavefaciens FD-1
    • Duncan, P. A., White, B. A. & Mackie, R. I. (1992). Purification and properties of NADP-dependent glutamate dehydrogenase from Ruminococcus flavefaciens FD-1. Appl Environ Microbiol 58, 4032-4037.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 4032-4037
    • Duncan, P.A.1    White, B.A.2    Mackie, R.I.3
  • 12
    • 0031027277 scopus 로고    scopus 로고
    • Cloning and characterisation of the Bacteroides fragilis metalloprotease toxin gene
    • Franco, A. A., Mundy, L. M., Trucksis, M., Wu, S., Kaper, J. B. & Sears, C. L. (1997). Cloning and characterisation of the Bacteroides fragilis metalloprotease toxin gene. Infect Immun 65, 1007-1013.
    • (1997) Infect Immun , vol.65 , pp. 1007-1013
    • Franco, A.A.1    Mundy, L.M.2    Trucksis, M.3    Wu, S.4    Kaper, J.B.5    Sears, C.L.6
  • 13
    • 0029030563 scopus 로고
    • Molecular analysis of surface-associated enzymes of Porphyromonas gingivalis
    • Gharbia, S. E. & Shah, H. N. (1995). Molecular analysis of surface-associated enzymes of Porphyromonas gingivalis. Clin Infect Dis 20, S160-166.
    • (1995) Clin Infect Dis , vol.20
    • Gharbia, S.E.1    Shah, H.N.2
  • 14
    • 0023883139 scopus 로고
    • Studies on the proteolytic activity of Bacteroides fragilis
    • Gibson, S. A. & Macfarlane, G. T. (1988a). Studies on the proteolytic activity of Bacteroides fragilis. J Gen Microbiol 134, 19-27.
    • (1988) J Gen Microbiol , vol.134 , pp. 19-27
    • Gibson, S.A.1    Macfarlane, G.T.2
  • 15
    • 0023759835 scopus 로고
    • Characterization of proteases formed by Bacteroides fragilis
    • Gibson, S. A. & Macfarlane, G. T. (1988b). Characterization of proteases formed by Bacteroides fragilis. J Gen Microbiol 134, 2231-2240.
    • (1988) J Gen Microbiol , vol.134 , pp. 2231-2240
    • Gibson, S.A.1    Macfarlane, G.T.2
  • 16
    • 0024252148 scopus 로고
    • +-glutamate dehydrogenase in Clostridium botulinum 113B
    • +-glutamate dehydrogenase in Clostridium botulinum 113B. Arch Microbiol 150, 460-464.
    • (1988) Arch Microbiol , vol.150 , pp. 460-464
    • Hammer, B.A.1    Johnson, E.A.2
  • 17
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S. (1984). Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28, 351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 18
    • 0003535096 scopus 로고
    • Blacksburg, VA: Virginia Polytechnic Institute and State University Anaerobe Laboratory
    • Holdeman, L. V. & Moore, W. E. C. (1972). Anaerobe Laboratory Manual, 4th edn. Blacksburg, VA: Virginia Polytechnic Institute and State University Anaerobe Laboratory.
    • (1972) Anaerobe Laboratory Manual, 4th Edn.
    • Holdeman, L.V.1    Moore, W.E.C.2
  • 19
    • 0024851296 scopus 로고
    • Molecular analysis of a novel glutamine synthetase of the anaerobe Bacteroides fragilis
    • corrigendum 136, 787
    • Hill, R. T., Parker, J. R., Goodman, H. J., Jones, D. T. & Woods, D. R. (1989). Molecular analysis of a novel glutamine synthetase of the anaerobe Bacteroides fragilis. J Gen Microbiol 135, 3271-3279 (corrigendum 136, 787).
    • (1989) J Gen Microbiol , vol.135 , pp. 3271-3279
    • Hill, R.T.1    Parker, J.R.2    Goodman, H.J.3    Jones, D.T.4    Woods, D.R.5
  • 20
    • 0019877072 scopus 로고
    • Rapid and efficient cosmid cloning
    • Ish-Horowicz, D. & Burke, J. F. (1981). Rapid and efficient cosmid cloning. Nucleic Acids Res 9, 2989-2998.
    • (1981) Nucleic Acids Res , vol.9 , pp. 2989-2998
    • Ish-Horowicz, D.1    Burke, J.F.2
  • 21
    • 0027198946 scopus 로고
    • Characterisation of recombinant and native forms of a cell surface antigen of Porphyromonas (Bacteroides) gingivalis
    • Joe, A., Yamamoto, A. & McBride, B. C. (1993). Characterisation of recombinant and native forms of a cell surface antigen of Porphyromonas (Bacteroides) gingivalis. Infect Immun 61, 3294-3303.
    • (1993) Infect Immun , vol.61 , pp. 3294-3303
    • Joe, A.1    Yamamoto, A.2    McBride, B.C.3
  • 22
    • 0028323014 scopus 로고
    • Nucleotide sequence of a Porphyromonas gingivalis gene encoding a surface-associated glutamate dehydrogenase and construction of a glutamate dehydrogenase-deficient isogenic mutant
    • Joe, A., Murray, C. S. & McBride, B. C. (1994). Nucleotide sequence of a Porphyromonas gingivalis gene encoding a surface-associated glutamate dehydrogenase and construction of a glutamate dehydrogenase-deficient isogenic mutant. Infect Immun 62, 1358-1368.
    • (1994) Infect Immun , vol.62 , pp. 1358-1368
    • Joe, A.1    Murray, C.S.2    McBride, B.C.3
  • 23
    • 0031024431 scopus 로고    scopus 로고
    • Cloning and characterisation of the gene for the metalloprotease enterotoxin of Bacteroides fragilis
    • Kling, J. J., Wright, R. L., Moncrief, J. S. & Wilkins, T. D. (1997). Cloning and characterisation of the gene for the metalloprotease enterotoxin of Bacteroides fragilis. FEMS Microbiol Lett 146, 279-284.
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 279-284
    • Kling, J.J.1    Wright, R.L.2    Moncrief, J.S.3    Wilkins, T.D.4
  • 24
    • 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 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0026063321 scopus 로고
    • Identification of the latex-reactive protein of Clostridium difficile as glutamate dehydrogenase
    • Lyerly, D., Barroso, L. A. & Wilkins, T. D. (1991). Identification of the latex-reactive protein of Clostridium difficile as glutamate dehydrogenase. J Clin Microbiol 29, 2639-2642.
    • (1991) J Clin Microbiol , vol.29 , pp. 2639-2642
    • Lyerly, D.1    Barroso, L.A.2    Wilkins, T.D.3
  • 26
    • 0026692792 scopus 로고
    • Synthesis and release of proteases by Bacteroides fragilis
    • Macfarlane, G. T., Macfarlane, S. & Gibson, S. A. W. (1993). Synthesis and release of proteases by Bacteroides fragilis. Curr Microbiol 24, 55-59.
    • (1993) Curr Microbiol , vol.24 , pp. 55-59
    • Macfarlane, G.T.1    Macfarlane, S.2    Gibson, S.A.W.3
  • 28
    • 0018599534 scopus 로고
    • Characterisation and mode of action of a bacteriocin produced by a Bacteroides fragilis strain
    • Mossie, K. G., Jones, D. T., Robb, F. T. & Woods, D. R. (1979). Characterisation and mode of action of a bacteriocin produced by a Bacteroides fragilis strain. Antimicrob Agents Chemother 16, 724-730.
    • (1979) Antimicrob Agents Chemother , vol.16 , pp. 724-730
    • Mossie, K.G.1    Jones, D.T.2    Robb, F.T.3    Woods, D.R.4
  • 29
    • 0000060736 scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine
    • Edited by F. C. Neidhardt, J. L. Ingraham, K. Brooks Low, B. Magasanik, M. Schlechter & H. E. Umbarger. Washington, DC: American Society for Microbiology
    • Reitzer, L. J. & Magasanik, B. (1987). Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine and D-alanine. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, pp. 302-320. Edited by F. C. Neidhardt, J. L. Ingraham, K. Brooks Low, B. Magasanik, M. Schlechter & H. E. Umbarger. Washington, DC: American Society for Microbiology.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 302-320
    • Reitzer, L.J.1    Magasanik, B.2
  • 30
    • 0018826669 scopus 로고
    • Effects of secreted Bacteroides proteases on the human intestinal brush border enzymes
    • Riepe, S. P., Goldstein, J. & Alpens, D. H. (1980). Effects of secreted Bacteroides proteases on the human intestinal brush border enzymes. J Clin Invest 66, 314-322.
    • (1980) J Clin Invest , vol.66 , pp. 314-322
    • Riepe, S.P.1    Goldstein, J.2    Alpens, D.H.3
  • 31
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg, M. & Court, D. (1979). Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet 13, 319-353.
    • (1979) Annu Rev Genet , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 32
    • 0003322065 scopus 로고
    • Reversible inactivation of glutamate dehydrogenase in Bacteroides fragilis: Purification and characterisation of high-activity and low-activity enzymes
    • Saito, H., Yamamoto, I. & Ishimoto, M. (1988). Reversible inactivation of glutamate dehydrogenase in Bacteroides fragilis: Purification and characterisation of high-activity and low-activity enzymes. J Gen Appl Microbiol 4, 377-385.
    • (1988) J Gen Appl Microbiol , vol.4 , pp. 377-385
    • Saito, H.1    Yamamoto, I.2    Ishimoto, M.3
  • 34
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., Nicklen, S. & Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74, 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 35
    • 0016154301 scopus 로고
    • The 3́-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to non-sense triplets and ribosome-binding sites
    • Shine, J. & Dalgarno, L. (1974). The 3́-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to non-sense triplets and ribosome-binding sites. Proc Natl Acad Sci USA 71, 1342-1346.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 36
    • 77956904836 scopus 로고
    • Glutamate dehydrogenases
    • Edited by P. D. Boyer. New York: Academic Press
    • Smith, E. L., Austen, B. M., Blumenthal, K. M. & Nyc, J. F. (1975). Glutamate dehydrogenases. In The Enzymes, vol. II, pp. 293-367. Edited by P. D. Boyer. New York: Academic Press.
    • (1975) The Enzymes , vol.2 , pp. 293-367
    • Smith, E.L.1    Austen, B.M.2    Blumenthal, K.M.3    Nyc, J.F.4
  • 37
    • 0022443220 scopus 로고
    • Expression and purification of glutamine synthetase cloned from Bacteroides fragilis
    • Southern, J. A., Parker, J. R. & Woods, D. R. (1986). Expression and purification of glutamine synthetase cloned from Bacteroides fragilis. J Gen Microbiol 132, 2827-2835.
    • (1986) J Gen Microbiol , vol.132 , pp. 2827-2835
    • Southern, J.A.1    Parker, J.R.2    Woods, D.R.3
  • 38
    • 0003318453 scopus 로고
    • Novel structure, properties and inactivation of glutamine synthetase from cloned Bacteroides fragilis
    • Southern, J. A., Parker, J. R. & Woods, D. R. (1987). Novel structure, properties and inactivation of glutamine synthetase from cloned Bacteroides fragilis. J Gen Microbiol 133, 2437-2446.
    • (1987) J Gen Microbiol , vol.133 , pp. 2437-2446
    • Southern, J.A.1    Parker, J.R.2    Woods, D.R.3
  • 39
    • 0026544783 scopus 로고
    • The glutamate dehydrogenase gene of Clostridium symbiosum: Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli
    • Teller, J. K., Smith, R. J., McPherson, M. J., Engel, P. C. & Guest, J. R. (1992). The glutamate dehydrogenase gene of Clostridium symbiosum: cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli. Eur J Biochem 206, 151-159.
    • (1992) Eur J Biochem , vol.206 , pp. 151-159
    • Teller, J.K.1    Smith, R.J.2    McPherson, M.J.3    Engel, P.C.4    Guest, J.R.5
  • 40
    • 0026504428 scopus 로고
    • Purification and characterisation of an enterotoxin from Bacteroides fragilis
    • Van Tassel, R. L., Lyerly, D. M. & Wilkins, T. D. (1992). Purification and characterisation of an enterotoxin from Bacteroides fragilis. Infect Immun 60, 1343-1350.
    • (1992) Infect Immun , vol.60 , pp. 1343-1350
    • Van Tassel, R.L.1    Lyerly, D.M.2    Wilkins, T.D.3
  • 41
    • 0016216108 scopus 로고
    • Nutritional features of Bacteroides fragilis subsp. fragilis
    • Varel, V. H. & Bryant, M. P. (1974). Nutritional features of Bacteroides fragilis subsp. fragilis. Appl Microbiol 28, 251-257.
    • (1974) Appl Microbiol , vol.28 , pp. 251-257
    • Varel, V.H.1    Bryant, M.P.2
  • 42
    • 0025364681 scopus 로고
    • Cloning of Bacteroides fragilis plasmid genes affecting metronidazole resistance and ultraviolet survival in Escherichia coli
    • Wehnert, G. U., Abratt, V. R., Goodman, H. J. K. & Woods, D. R. (1990). Cloning of Bacteroides fragilis plasmid genes affecting metronidazole resistance and ultraviolet survival in Escherichia coli. Plasmid 23, 155-158.
    • (1990) Plasmid , vol.23 , pp. 155-158
    • Wehnert, G.U.1    Abratt, V.R.2    Goodman, H.J.K.3    Woods, D.R.4
  • 43
    • 0029758538 scopus 로고    scopus 로고
    • The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth
    • Wen, Z. & Morrison, M. (1996). The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth. Appl Environ Microbiol 62, 3826-3833.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3826-3833
    • Wen, Z.1    Morrison, M.2
  • 44
    • 0030851473 scopus 로고    scopus 로고
    • Glutamate dehydrogenase activity profiles for type strains of ruminal Prevotella spp
    • Wen, Z. & Morrison, M. (1997). Glutamate dehydrogenase activity profiles for type strains of ruminal Prevotella spp. Appl Environ Microbiol 63, 3314-3317.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3314-3317
    • Wen, Z.1    Morrison, M.2
  • 45
    • 0021590858 scopus 로고
    • The pathway of ammonia assimilation in Bacteroides fragilis
    • Yamamoto, I., Abe, A., Saito, H. & Ishimoto, M. (1984). The pathway of ammonia assimilation in Bacteroides fragilis. J Gen Appl Microbiol 30, 499-508.
    • (1984) J Gen Appl Microbiol , vol.30 , pp. 499-508
    • Yamamoto, I.1    Abe, A.2    Saito, H.3    Ishimoto, M.4
  • 46
    • 0023355295 scopus 로고
    • Properties of glutamate dehydrogenase purified from Bacteroides fragilis
    • Yamamoto, I., Abe, A. & Ishimoto, M. (1987a). Properties of glutamate dehydrogenase purified from Bacteroides fragilis. J Biochem (Tokyo) 101, 1391-1397.
    • (1987) J Biochem (Tokyo) , vol.101 , pp. 1391-1397
    • Yamamoto, I.1    Abe, A.2    Ishimoto, M.3
  • 47
    • 18344404611 scopus 로고
    • Regulation of synthesis and reversible inactivation in vivo of dual coenzyme-specific glutamate dehydrogenase in Bacteroides fragilis
    • Yamamoto, I., Saito, H. & Ishimoto, M. (1987b). Regulation of synthesis and reversible inactivation in vivo of dual coenzyme-specific glutamate dehydrogenase in Bacteroides fragilis. J Gen Microbiol 133, 2773-2780.
    • (1987) J Gen Microbiol , vol.133 , pp. 2773-2780
    • Yamamoto, I.1    Saito, H.2    Ishimoto, M.3
  • 48
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 49
    • 0020338572 scopus 로고
    • Enhanced expression of croβ-galactosidase fusion proteins under the control of the Pr promoter of bacteriophage lambda
    • Zabeau, M. & Stanley, K. K. (1982). Enhanced expression of croβ-galactosidase fusion proteins under the control of the Pr promoter of bacteriophage lambda. EMBO J 1, 1217-1224.
    • (1982) EMBO J , vol.1 , pp. 1217-1224
    • Zabeau, M.1    Stanley, K.K.2


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