메뉴 건너뛰기




Volumn 66, Issue 6, 2000, Pages 2502-2512

Bile salt hydrolase of Bifidobacterium longum - Biochemical and genetic characterization

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HYDROLASE;

EID: 0034048222     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.6.2502-2512.2000     Document Type: Article
Times cited : (242)

References (57)
  • 2
    • 0001872327 scopus 로고    scopus 로고
    • Bifidobacteria and probiotic action
    • S. Salminen and A. Von Wright (ed.). Marcel Dekker, Inc., New York, N.Y.
    • Ballongue, J. 1998. Bifidobacteria and probiotic action, p. 519-587. In S. Salminen and A. Von Wright (ed.), Lactic acid bacteria. Microbiology and functional aspects. Marcel Dekker, Inc., New York, N.Y.
    • (1998) Lactic Acid Bacteria. Microbiology and Functional Aspects , pp. 519-587
    • Ballongue, J.1
  • 3
    • 0013096875 scopus 로고
    • An improved medium for lactobacilli
    • Briggs, M. 1953. An improved medium for lactobacilli. J. Dairy Res. 20:36-40.
    • (1953) J. Dairy Res. , vol.20 , pp. 36-40
    • Briggs, M.1
  • 4
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G., J. Kok, K. J. Leenhouts, M. Dabrowska, G. Venema, and A. J. Haandrikman. 1995. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 177:1554-1563.
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 5
    • 0023414693 scopus 로고
    • Deconjugation of bile acids by human intestinal bacteria implanted in germ-free rats
    • Chikai, T., H. Nakao, and K. Uchida. 1987. Deconjugation of bile acids by human intestinal bacteria implanted in germ-free rats. Lipids 22:669-671.
    • (1987) Lipids , vol.22 , pp. 669-671
    • Chikai, T.1    Nakao, H.2    Uchida, K.3
  • 6
    • 0026446050 scopus 로고
    • Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay
    • Christiaens, H., R. J. Leer, P. H. Pouwels, and W. Verstraete. 1992. Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay. Appl. Environ. Microbiol. 58:3792-3798.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3792-3798
    • Christiaens, H.1    Leer, R.J.2    Pouwels, P.H.3    Verstraete, W.4
  • 7
    • 0029041833 scopus 로고
    • Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens
    • Coleman, J. P., and L. L. Hudson. 1995. Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens. Appl. Environ. Microbiol. 61:2514-2520.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2514-2520
    • Coleman, J.P.1    Hudson, L.L.2
  • 8
    • 0031892684 scopus 로고    scopus 로고
    • Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity
    • De Smet, I., P. DeBoever, and W. Verstraete. 1998. Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity. Br. J. Nutr. 79:185-194.
    • (1998) Br. J. Nutr. , vol.79 , pp. 185-194
    • De Smet, I.1    DeBoever, P.2    Verstraete, W.3
  • 9
    • 0028254682 scopus 로고
    • In vitro study of bile salt hydrolase (BSH) activity of BSH isogenic Lactobacillus plantarum 80 strains and estimation of cholesterol lowering through enhanced BSH activity
    • De Smet, I., L. Van Hoorde, N. De Saeyer, M. Vande Woestyne, and W. Verstraete. 1994. In vitro study of bile salt hydrolase (BSH) activity of BSH isogenic Lactobacillus plantarum 80 strains and estimation of cholesterol lowering through enhanced BSH activity. Microb. Ecol. Health Dis. 7:315-329.
    • (1994) Microb. Ecol. Health Dis. , vol.7 , pp. 315-329
    • De Smet, I.1    Van Hoorde, L.2    De Saeyer, N.3    Woestyne, M.V.4    Verstraete, W.5
  • 11
    • 0031720810 scopus 로고    scopus 로고
    • Identification of genes encoding conjugated bile salt hydrolase and transport in Lactobacillus johnsonii 100-100
    • Elkins, C. A., and D. C. Savage. 1998. Identification of genes encoding conjugated bile salt hydrolase and transport in Lactobacillus johnsonii 100-100. J. Bacteriol. 180:4344-4349.
    • (1998) J. Bacteriol. , vol.180 , pp. 4344-4349
    • Elkins, C.A.1    Savage, D.C.2
  • 13
    • 0024058679 scopus 로고
    • Purification and characterization of bile salt hydrolase from Clostridium perfringens
    • Gopal-Srivastava, R., and P. B. Hylemon. 1988. Purification and characterization of bile salt hydrolase from Clostridium perfringens. J. Lipid Res. 29:1079-1085.
    • (1988) J. Lipid Res. , vol.29 , pp. 1079-1085
    • Gopal-Srivastava, R.1    Hylemon, P.B.2
  • 14
    • 0020580289 scopus 로고
    • Sequence diversity among related genes for recognition of specific targets in DNA molecules
    • Gough, J. A., and N. E. Murray. 1983. Sequence diversity among related genes for recognition of specific targets in DNA molecules. J. Mol. Biol. 166:1-19.
    • (1983) J. Mol. Biol. , vol.166 , pp. 1-19
    • Gough, J.A.1    Murray, N.E.2
  • 15
    • 0029063548 scopus 로고
    • Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536
    • Grill, J. P., F. Schneider, J. Crociani, and J. Ballongue. 1995. Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536. Appl. Environ. Microbiol. 61:2577-2582.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2577-2582
    • Grill, J.P.1    Schneider, F.2    Crociani, J.3    Ballongue, J.4
  • 16
    • 0025096383 scopus 로고
    • Chemical species of lipids in bile
    • Hay, D. W., and M. C. Carey. 1990. Chemical species of lipids in bile. Hepatology 12:6S-14S.
    • (1990) Hepatology , vol.12
    • Hay, D.W.1    Carey, M.C.2
  • 17
    • 0001959474 scopus 로고
    • Strategies in regulation of transcription initiation
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.). American Society for Microbiology, Washington, D.C.
    • Hoopes, B. C., and W. R. McClure. 1987. Strategies in regulation of transcription initiation, p. 1231-1240. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , pp. 1231-1240
    • Hoopes, B.C.1    McClure, W.R.2
  • 18
    • 0020029418 scopus 로고
    • Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora
    • Huijghebaert, S. M., J. A. Mertens, and H. J. Eyssen. 1982. Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora. Appl. Environ. Microbiol. 43:185-192.
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 185-192
    • Huijghebaert, S.M.1    Mertens, J.A.2    Eyssen, H.J.3
  • 19
    • 0002007302 scopus 로고    scopus 로고
    • Genetic modification of intestinal lactobacilli and bifidobacteria
    • G. W. Tannock (ed.). Horizon Scientific Press, Norfolk, United Kingdom
    • Kullen, M. J., and T.-R. Klaenhammer. 1999. Genetic modification of intestinal lactobacilli and bifidobacteria, p. 65-83. In G. W. Tannock (ed.), Probiotics. A critical review. Horizon Scientific Press, Norfolk, United Kingdom.
    • (1999) Probiotics. A Critical Review , pp. 65-83
    • Kullen, M.J.1    Klaenhammer, T.-R.2
  • 20
    • 0001620865 scopus 로고
    • The health potential of products containing bifidobacteria
    • R. K. Robinson (ed.). Elsevier Applied Science, London, United Kingdom
    • Kurmann, J. A., and J. L. Rasic. 1991. The health potential of products containing bifidobacteria, p. 117-157. In R. K. Robinson (ed.), Therapeutic properties of fermented milks. Elsevier Applied Science, London, United Kingdom.
    • (1991) Therapeutic Properties of Fermented Milks , pp. 117-157
    • Kurmann, J.A.1    Rasic, J.L.2
  • 21
    • 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
  • 22
    • 13144263158 scopus 로고
    • An improved colorimetric determination of amino acids with the use of ninhydrin
    • Lee, Y. P., and T. Takahashi. 1966. An improved colorimetric determination of amino acids with the use of ninhydrin. Anal. Biochem. 14:71-77.
    • (1966) Anal. Biochem. , vol.14 , pp. 71-77
    • Lee, Y.P.1    Takahashi, T.2
  • 23
    • 0024618913 scopus 로고
    • Campbell-like integration of heterologous plasmid DNA into the chromosome of Lactococcus lactis
    • Leenhouts, K. J., J. Kok, and G. Venema. 1989. Campbell-like integration of heterologous plasmid DNA into the chromosome of Lactococcus lactis. Appl. Environ. Microbiol. 55:394-400.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 394-400
    • Leenhouts, K.J.1    Kok, J.2    Venema, G.3
  • 24
    • 0027174276 scopus 로고
    • Gene disruption in Lactobacillus plantarum strain 80 by site-specific recombination: Isolation of a mutant strain deficient in conjugated bile salt hydrolase activity
    • Leer, R. J., H. Christiaens, W. Verstraete, L. Peters, M. Posno, and P. H. Pouwels. 1993. Gene disruption in Lactobacillus plantarum strain 80 by site-specific recombination: isolation of a mutant strain deficient in conjugated bile salt hydrolase activity. Mol. Gen. Genet. 239:269-272.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 269-272
    • Leer, R.J.1    Christiaens, H.2    Verstraete, W.3    Peters, L.4    Posno, M.5    Pouwels, P.H.6
  • 25
    • 0025348851 scopus 로고
    • Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100
    • Lundeen, S. G., and D. C. Savage. 1990. Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100. J. Bacteriol. 172: 4171-4177.
    • (1990) J. Bacteriol. , vol.172 , pp. 4171-4177
    • Lundeen, S.G.1    Savage, D.C.2
  • 26
    • 0026574594 scopus 로고
    • Multiple forms of bile salt hydrolase from Lactobacillus sp. strain 100-100
    • Lundeen, S. G., and D. C. Savage. 1992. Multiple forms of bile salt hydrolase from Lactobacillus sp. strain 100-100. J. Bacteriol. 174:7217-7220.
    • (1992) J. Bacteriol. , vol.174 , pp. 7217-7220
    • Lundeen, S.G.1    Savage, D.C.2
  • 27
    • 0027449947 scopus 로고
    • The regulation of nitrogen utilization in enteric bacteria
    • Magasanik, B. 1993. The regulation of nitrogen utilization in enteric bacteria. J. Cell. Biochem. 51:34-40.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 34-40
    • Magasanik, B.1
  • 29
    • 0027326261 scopus 로고
    • Potential of using lactic acid bacteria for therapy and immunomodulation in man
    • Marteau, P., and J. C. Rambaud. 1993. Potential of using lactic acid bacteria for therapy and immunomodulation in man. FEMS Microbiol. Rev. 12:207-220.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 207-220
    • Marteau, P.1    Rambaud, J.C.2
  • 30
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262: 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 31
    • 0024806266 scopus 로고
    • Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: A new feature of the allosteric site
    • Minowa, T., S. Iwata, H. Sakai, H. Masaki, and T. Ohta. 1989. Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site. Gene 85:161-168.
    • (1989) Gene , vol.85 , pp. 161-168
    • Minowa, T.1    Iwata, S.2    Sakai, H.3    Masaki, H.4    Ohta, T.5
  • 33
    • 0039001059 scopus 로고
    • Improved double-stranded DNA sequencing using the linear polymerase chain reaction
    • Murray, V. 1989. Improved double-stranded DNA sequencing using the linear polymerase chain reaction. Nucleic Acids Res. 17:8889.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8889
    • Murray, V.1
  • 34
    • 0015847127 scopus 로고
    • Postprandial concentrations of free and conjugated bile acids down the length of the normal human small intestine
    • Northfield, T. C., and I. McColl. 1973. Postprandial concentrations of free and conjugated bile acids down the length of the normal human small intestine. Gut 14:513-518.
    • (1973) Gut , vol.14 , pp. 513-518
    • Northfield, T.C.1    McColl, I.2
  • 35
    • 0030426625 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the β-D-glucosidase gene from Bifidobacterium breve clb, and expression of β-D-glucosidase activity in Escherichia coli
    • Nunoura, N., K. Ohdan, K. Tanaka, H. Tamaki, T. Yano, M. Inui, H. Yukawa, K. Yamamoto, and H. Kumagai. 1996. Cloning and nucleotide sequence of the β-D-glucosidase gene from Bifidobacterium breve clb, and expression of β-D-glucosidase activity in Escherichia coli. Biosci. Biotechnol. Biochem. 60:2011-2018.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 2011-2018
    • Nunoura, N.1    Ohdan, K.2    Tanaka, K.3    Tamaki, H.4    Yano, T.5    Inui, M.6    Yukawa, H.7    Yamamoto, K.8    Kumagai, H.9
  • 36
    • 0023013740 scopus 로고
    • Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericus
    • Olsson, A., and M. Uhlén. 1986. Sequencing and heterologous expression of the gene encoding penicillin V amidase from Bacillus sphaericus. Gene 45:175-181.
    • (1986) Gene , vol.45 , pp. 175-181
    • Olsson, A.1    Uhlén, M.2
  • 37
    • 0014730653 scopus 로고
    • Genetic and transfection studies with Bacillus subtilis phage SP50
    • Rottlander, E., and T. A. Trautner. 1970. Genetic and transfection studies with Bacillus subtilis phage SP50. J. Mol. Biol. 108:47-60.
    • (1970) J. Mol. Biol. , vol.108 , pp. 47-60
    • Rottlander, E.1    Trautner, T.A.2
  • 39
    • 0001345442 scopus 로고
    • The genus Bifidobacterium
    • B. J. B. Wood and W. H. Holzapfel (ed.). Blackie Academic & Professional, London, United Kingdom
    • Sgorbati, B., B. Biavati, and D. Palenzona. 1995. The genus Bifidobacterium, p. 279-306. In B. J. B. Wood and W. H. Holzapfel (ed.), The genera of lactic acid bacteria. Blackie Academic & Professional, London, United Kingdom.
    • (1995) The Genera of Lactic Acid Bacteria , pp. 279-306
    • Sgorbati, B.1    Biavati, B.2    Palenzona, D.3
  • 40
    • 0025239461 scopus 로고
    • Physical-chemical behavior of dietary and biliary lipids during intestinal digestion and absorption. 1. Phase behavior and aggregation states of model lipid systems patterned after aqueous duodenal contents of healthy adult human beings
    • Staggers, J. E., O. Hernell, R. J. Stafford, and M. C. Carey. 1990. Physical-chemical behavior of dietary and biliary lipids during intestinal digestion and absorption. 1. Phase behavior and aggregation states of model lipid systems patterned after aqueous duodenal contents of healthy adult human beings. Biochemistry 29:2028-2040.
    • (1990) Biochemistry , vol.29 , pp. 2028-2040
    • Staggers, J.E.1    Hernell, O.2    Stafford, R.J.3    Carey, M.C.4
  • 41
    • 0017110325 scopus 로고
    • Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis
    • Stellwag, E. J., and P. B. Hylemon. 1976. Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452:165-176.
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 165-176
    • Stellwag, E.J.1    Hylemon, P.B.2
  • 43
    • 0006962619 scopus 로고
    • Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I
    • Tabor, S., and C. C. Richardson. 1989. Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I. Proc. Natl. Acad. Sci. USA 86:4076-4080.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4076-4080
    • Tabor, S.1    Richardson, C.C.2
  • 44
    • 0033251402 scopus 로고    scopus 로고
    • Screening of lactic acid bacteria for bile salt hydrolase activity
    • Tanaka, H., K. Doesburg, T. Iwasaki, and I. Mierau. 1999. Screening of lactic acid bacteria for bile salt hydrolase activity. J. Dairy Sci. 82:2530-2535.
    • (1999) J. Dairy Sci. , vol.82 , pp. 2530-2535
    • Tanaka, H.1    Doesburg, K.2    Iwasaki, T.3    Mierau, I.4
  • 45
    • 0000540595 scopus 로고
    • Microecology of the gastrointestinal tract in relation to lactic acid bacteria
    • Tannock, G. W. 1995. Microecology of the gastrointestinal tract in relation to lactic acid bacteria. Int. Dairy J. 5:1059-1070.
    • (1995) Int. Dairy J. , vol.5 , pp. 1059-1070
    • Tannock, G.W.1
  • 46
    • 0030896599 scopus 로고    scopus 로고
    • Effect of sodium taurocholate on the in vitro growth of lactobacilli
    • Tannock, G. W., J. M. Bateup, and H. F. Jenkinson. 1997. Effect of sodium taurocholate on the in vitro growth of lactobacilli. Microb. Ecol. 33:163-167.
    • (1997) Microb. Ecol. , vol.33 , pp. 163-167
    • Tannock, G.W.1    Bateup, J.M.2    Jenkinson, H.F.3
  • 48
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi, B. E., and W. Sandine. 1975. Improved medium for lactic streptococci and their bacteriophages. Appl. Environ. Microbiol. 29:807-813.
    • (1975) Appl. Environ. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.2
  • 49
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 50
    • 0027462187 scopus 로고
    • Cloning, nucleotide sequence, and regulatory analysis of the Lactococcus lactis dnaJ gene
    • van Asseldonk, M., A. Simons, H. Visser, W. M. De Vos, and G. Simons. 1993. Cloning, nucleotide sequence, and regulatory analysis of the Lactococcus lactis dnaJ gene. J. Bacteriol. 175:1537-1644.
    • (1993) J. Bacteriol. , vol.175 , pp. 1537-1644
    • Van Asseldonk, M.1    Simons, A.2    Visser, H.3    De Vos, W.M.4    Simons, G.5
  • 52
    • 0023780027 scopus 로고
    • Isolation and identification of intestinal steroid-desulfating bacteria from rats and humans
    • Van Eldere, J., J. Robben, G. De Pauw, R. Merckx, and H. Eyssen. 1988. Isolation and identification of intestinal steroid-desulfating bacteria from rats and humans. Appl. Environ. Microbiol. 54:2112-2117.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2112-2117
    • Van Eldere, J.1    Robben, J.2    De Pauw, G.3    Merckx, R.4    Eyssen, H.5
  • 53
    • 0027281747 scopus 로고
    • The genes of the glutamine synthetase adenylation cascade are not regulated by nitrogen in Escherichia coli
    • van Heeswijk, W. C., M. Rabenberg, H. V. Westerhoff, and D. Kahn. 1993. The genes of the glutamine synthetase adenylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9:443-457.
    • (1993) Mol. Microbiol. , vol.9 , pp. 443-457
    • Van Heeswijk, W.C.1    Rabenberg, M.2    Westerhoff, H.V.3    Kahn, D.4
  • 55
    • 0025809486 scopus 로고
    • New pUC derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and J. Messing. 1991. New pUC derived cloning vectors with different selectable markers and DNA replication origins. Gene 100:189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 56
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 57
    • 0025084949 scopus 로고
    • High efficiency electroporation of ligated DNA into bacteria
    • Zabarovsky, E. R., and G. Winberg. 1990. High efficiency electroporation of ligated DNA into bacteria. Nucleic Acids Res. 18:912.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 912
    • Zabarovsky, E.R.1    Winberg, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.