메뉴 건너뛰기




Volumn 12, Issue 1, 1996, Pages 31-39

Intracellular expression of Vitreoscilla hemoglobin (VHb) enhances total protein secretion and improves the production of α-amylase and neutral protease in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BATCH CELL CULTURE; BIOASSAY; BIOREACTORS; CELLS; ENZYME KINETICS; ENZYMES; GENES; GROWTH KINETICS;

EID: 0030038319     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp950065j     Document Type: Article
Times cited : (63)

References (60)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C.; Spizizen, J. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 1961, 169, 324-333.
    • (1961) J. Bacteriol. , vol.169 , pp. 324-333
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 2
    • 0002568699 scopus 로고
    • Fermentation of Bacillus
    • Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC
    • Arbige, M. V.; Bulthuis, B. A.; Schultz, J.; Crabb, D. Fermentation of Bacillus. In Bacillus subtilis and other gram-positive bacteria; Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC, 1993; pp 871-895.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 871-895
    • Arbige, M.V.1    Bulthuis, B.A.2    Schultz, J.3    Crabb, D.4
  • 3
    • 0027354948 scopus 로고
    • Host-vector interactions in Escherichia coli
    • Bailey, J. E. Host-vector interactions in Escherichia coli. Adv. Biochem. Eng./Biotechnol. 1993, 48, 29-52.
    • (1993) Adv. Biochem. Eng./Biotechnol. , vol.48 , pp. 29-52
    • Bailey, J.E.1
  • 4
    • 0021592145 scopus 로고
    • Bacillus subtilis requires a "stringent" Shine-Dalgarno region for gene expression
    • Band, L.; Henner, D. J. Bacillus subtilis requires a "stringent" Shine-Dalgarno region for gene expression. DNA 1984, 3, 17-21.
    • (1984) DNA , vol.3 , pp. 17-21
    • Band, L.1    Henner, D.J.2
  • 6
    • 0002711149 scopus 로고
    • Production of Bacillus thuringiensis insecticides for experimental and commercial uses
    • Entwistle, P. F., Cory, J. S., Bailey, M. J., Higgs, S., Eds.; John Wiley & Sons Ltd: England
    • Bernhard, K.; Utz, R. Production of Bacillus thuringiensis insecticides for experimental and commercial uses. In Bacillus thuringiensis, an environmental biopesticide: Theory and practice; Entwistle, P. F., Cory, J. S., Bailey, M. J., Higgs, S., Eds.; John Wiley & Sons Ltd: England, 1993; pp 255-267.
    • (1993) Bacillus Thuringiensis, An Environmental Biopesticide: Theory and Practice , pp. 255-267
    • Bernhard, K.1    Utz, R.2
  • 7
    • 0025960282 scopus 로고
    • Effect of signal sequence alteration on expression of levansucrase in Bacillus subtilis
    • Borchert, T. V.; Nagarajan, V. Effect of signal sequence alteration on expression of levansucrase in Bacillus subtilis. J. Bacteriol. 1991, 173, 276-282.
    • (1991) J. Bacteriol. , vol.173 , pp. 276-282
    • Borchert, T.V.1    Nagarajan, V.2
  • 8
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0025964291 scopus 로고
    • The initiation of sporulation in Bacillus subtilis is controlled by a multicomponent phosphorelay
    • Burbulys, D.; Trach, K. A.; Hoch, J. A. The initiation of sporulation in Bacillus subtilis is controlled by a multicomponent phosphorelay. Cell 1991, 64, 545-552.
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 10
    • 0028465483 scopus 로고
    • 31P NMR and saturation transfer study
    • 31P NMR and saturation transfer study. Biotechnol. Prog. 1994, 10, 360-364.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 360-364
    • Chen, R.1    Bailey, J.E.2
  • 11
    • 0028430975 scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin alters aerobic metabolism of Saccharomyces cerevisiae
    • Chen, W.; Hughes, D. E.; Bailey, J. E. Intracellular expression of Vitreoscilla hemoglobin alters aerobic metabolism of Saccharomyces cerevisiae. Biotechnol. Prog. 1994, 10, 308-313.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 308-313
    • Chen, W.1    Hughes, D.E.2    Bailey, J.E.3
  • 12
    • 0025783281 scopus 로고
    • Separate promoters direct expression of phoAIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation
    • Chesnut, R. S.; Bookstein, C.; Hulett, F. M. Separate promoters direct expression of phoAIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation. Mol. Microbiol. 1991, 5, 2181-2190.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2181-2190
    • Chesnut, R.S.1    Bookstein, C.2    Hulett, F.M.3
  • 13
    • 0016440133 scopus 로고
    • Production and possible function of serine protease during sporulation of Bacillus subtilis
    • Dancer, B. N.; Mandelstam, J. Production and possible function of serine protease during sporulation of Bacillus subtilis. J. Bacteriol. 1975, 121, 406-410.
    • (1975) J. Bacteriol. , vol.121 , pp. 406-410
    • Dancer, B.N.1    Mandelstam, J.2
  • 14
    • 0000220903 scopus 로고
    • Production of nucleotides by microorganisms
    • Rose, A.-H., Ed.; Academic Press: New York
    • Demain, A. L. Production of nucleotides by microorganisms. In Economic microbiology: Primary products of metabolism; Rose, A.-H., Ed.; Academic Press: New York, 1978; Vol. 2, pp 187-208.
    • (1978) Economic Microbiology: Primary Products of Metabolism , vol.2 , pp. 187-208
    • Demain, A.L.1
  • 16
    • 0025353062 scopus 로고
    • A. Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcription fusion
    • Dikshit, K. L.; Dikshit, R. P.; Webster, D. A. Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcription fusion. Nucleic Acid Res. 1990, 18, 4149-4155.
    • (1990) Nucleic Acid Res. , vol.18 , pp. 4149-4155
    • Dikshit, K.L.1    Dikshit, R.P.2    Webster, D.3
  • 17
    • 0001949658 scopus 로고
    • Commercial production of extracellular enzymes
    • Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC
    • Ferrari, E.; Jarnagin, A. S.; Schmidt, B. F. Commercial production of extracellular enzymes. In Bacillus subtilis and other gram-positive bacteria; Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC, 1993; pp 917-937.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 917-937
    • Ferrari, E.1    Jarnagin, A.S.2    Schmidt, B.F.3
  • 18
    • 0026609393 scopus 로고
    • Protein secretion in gram-positive bacteria
    • Freudl, R. Protein secretion in gram-positive bacteria. J. Biotechnol. 1992, 23, 231-240.
    • (1992) J. Biotechnol. , vol.23 , pp. 231-240
    • Freudl, R.1
  • 19
    • 0023410779 scopus 로고
    • The effect of restriction shotgun cloning and plasmid stability in Bacillus subtilis Marburg
    • Haima, P.; Bron, S.; Venema, G. The effect of restriction shotgun cloning and plasmid stability in Bacillus subtilis Marburg. Mol. Gen. Genet. 1987, 209, 335-342.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 335-342
    • Haima, P.1    Bron, S.2    Venema, G.3
  • 20
    • 0025021166 scopus 로고
    • Development of a β-galactosidase α-complementation system for molecular cloning in Bacillus subtilis
    • Haima, P.; Van Sinderen, D.; Schotting, H.; Bron, S.; Venema, G. Development of a β-galactosidase α-complementation system for molecular cloning in Bacillus subtilis. Gene 1990, 86, 63-69.
    • (1990) Gene , vol.86 , pp. 63-69
    • Haima, P.1    Van Sinderen, D.2    Schotting, H.3    Bron, S.4    Venema, G.5
  • 21
    • 0025285066 scopus 로고
    • Inducible expression of regulatory genes in Bacillus subtilis
    • Henner, D. J. Inducible expression of regulatory genes in Bacillus subtilis. Methods Enzymol. 1990, 185, 223-228.
    • (1990) Methods Enzymol. , vol.185 , pp. 223-228
    • Henner, D.J.1
  • 22
    • 0022379739 scopus 로고
    • Construction of a secretion vector containing the preprostructure coding region of Bacillus amyloliquefaciens neutral protease gene and secretion of Bacillus subtilis α-amylase and human interferon-beta in Bacillus subtilis
    • Honjo, M.; Akaoka, A.; Nakayama, A.; Shimada, H.; Furutani, Y. Construction of a secretion vector containing the preprostructure coding region of Bacillus amyloliquefaciens neutral protease gene and secretion of Bacillus subtilis α-amylase and human interferon-beta in Bacillus subtilis. J. Biotechnol. 1985, 3, 73-84.
    • (1985) J. Biotechnol. , vol.3 , pp. 73-84
    • Honjo, M.1    Akaoka, A.2    Nakayama, A.3    Shimada, H.4    Furutani, Y.5
  • 23
    • 0022760316 scopus 로고
    • The effect of the inverted repeat structure on the production of the cloned Bacillus amyloliquefaciens α-amylase
    • Kallio, P. The effect of the inverted repeat structure on the production of the cloned Bacillus amyloliquefaciens α-amylase. Eur. J. Biochem. 1986, 158, 491-495.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 491-495
    • Kallio, P.1
  • 24
    • 0005893052 scopus 로고
    • Enhancement of α-amylase production by integrating and amplifying the α-amylase gene of Bacillus amyloliquefaciens in the genome of Bacillus subtilis
    • Kallio, P.; Palva, A.; Palva, I. Enhancement of α-amylase production by integrating and amplifying the α-amylase gene of Bacillus amyloliquefaciens in the genome of Bacillus subtilis. Appl. Microbiol. Biotechnol. 1987, 27, 64-71.
    • (1987) Appl. Microbiol. Biotechnol. , vol.27 , pp. 64-71
    • Kallio, P.1    Palva, A.2    Palva, I.3
  • 25
    • 0025915507 scopus 로고
    • The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein
    • Kallio, P. T.; Fagelson, J. E.; Hoch, J. A.; Strauch, M. A. The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein. J. Biol. Chem. 1991, 266, 13411-13417.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13411-13417
    • Kallio, P.T.1    Fagelson, J.E.2    Hoch, J.A.3    Strauch, M.A.4
  • 26
    • 0027976409 scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin alters Escherichia coli energy metabolism under oxygen-limited conditions
    • Kallio, P. T.; Kim, D. J.; Tsai, P. S.; Bailey, J. E. Intracellular expression of Vitreoscilla hemoglobin alters Escherichia coli energy metabolism under oxygen-limited conditions. Eur. J. Biochem. 1994, 219, 201-208.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 201-208
    • Kallio, P.T.1    Kim, D.J.2    Tsai, P.S.3    Bailey, J.E.4
  • 27
    • 0025670272 scopus 로고
    • The Bacillus subtilis phoAIV gene: Effects of in vitro inactivation on total alkaline phosphatase production
    • Kapp, N. V.; Edwards, C. W.; Chesnut, R. S.; Hulett, F. M. The Bacillus subtilis phoAIV gene: effects of in vitro inactivation on total alkaline phosphatase production. Gene 1990, 96, 95-100.
    • (1990) Gene , vol.96 , pp. 95-100
    • Kapp, N.V.1    Edwards, C.W.2    Chesnut, R.S.3    Hulett, F.M.4
  • 28
    • 0023874286 scopus 로고
    • Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli
    • Khosla, C.; Bailey, J. E. Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 1988, 331, 633-635.
    • (1988) Nature , vol.331 , pp. 633-635
    • Khosla, C.1    Bailey, J.E.2
  • 29
    • 0025050682 scopus 로고
    • Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli
    • Khosla, C.; Curtis, J. E.; DeModena, J.; Rinas, U.; Bailey, J. E. Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli. Bio/Technology 1990, 8, 849-853.
    • (1990) Bio/Technology , vol.8 , pp. 849-853
    • Khosla, C.1    Curtis, J.E.2    Demodena, J.3    Rinas, U.4    Bailey, J.E.5
  • 30
    • 0025645664 scopus 로고
    • Presence of the bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain
    • Khosravi, M.; Webster, D. A.; Stark, B. C. Presence of the bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain. Plasmid 1990, 24, 190-194.
    • (1990) Plasmid , vol.24 , pp. 190-194
    • Khosravi, M.1    Webster, D.A.2    Stark, B.C.3
  • 31
    • 4444340148 scopus 로고
    • Non-ribosomal peptide formation on multifunctional proteins
    • Kleinkauf, H.; von Dohren, H, Non-ribosomal peptide formation on multifunctional proteins. Trends Biochem. Sci. 1983, 8, 281-283.
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 281-283
    • Kleinkauf, H.1    Von Dohren, H.2
  • 32
    • 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 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0025828687 scopus 로고
    • Bacillus subtilis expresses two kinds of haem A-containing terminal oxidases
    • Laureus, M.; Haltia, T.; Saraste, M.; Wikström, M. Bacillus subtilis expresses two kinds of haem A-containing terminal oxidases. Eur. J. Biochem. 1991, 197, 699-705.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 699-705
    • Laureus, M.1    Haltia, T.2    Saraste, M.3    Wikström, M.4
  • 34
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1955, 1, 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 35
    • 14744278506 scopus 로고
    • Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by expression of a bacterial hemoglobin
    • Magnolo, S. K.; Leenutaphong, D. L.; DeModena, J. A.; Curtis, J. E.; Bailey, J. E.; Galazzo, J. L.; Hughes, D. E. Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by expression of a bacterial hemoglobin. Bio/Technology 1991, 9, 473-476.
    • (1991) Bio/Technology , vol.9 , pp. 473-476
    • Magnolo, S.K.1    Leenutaphong, D.L.2    DeModena, J.A.3    Curtis, J.E.4    Bailey, J.E.5    Galazzo, J.L.6    Hughes, D.E.7
  • 37
    • 0022409380 scopus 로고
    • Export of α-amylase by Bacillus amyloliquefaciens requires proton motive force
    • Muren, E. M.; Randall, L. Export of α-amylase by Bacillus amyloliquefaciens requires proton motive force. J. Bacteriol. 1985, 164, 712-716.
    • (1985) J. Bacteriol. , vol.164 , pp. 712-716
    • Muren, E.M.1    Randall, L.2
  • 38
    • 0001914212 scopus 로고
    • Protein secretion
    • Sonnenshein, A. L., Hoch., J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC
    • Nagarajan, V. Protein secretion. In Bacillus subtilis and other gram-positive bacteria; Sonnenshein, A. L., Hoch., J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC, 1993; pp 713-726.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 713-726
    • Nagarajan, V.1
  • 39
    • 0022480721 scopus 로고
    • Secretion of a heterologous protein from Bacillus subtilis with the aid of protease signal sequences
    • Nagarajan, V.; Thompson, L. D. Secretion of a heterologous protein from Bacillus subtilis with the aid of protease signal sequences. J. Bacteriol. 1986, 165, 837-842.
    • (1986) J. Bacteriol. , vol.165 , pp. 837-842
    • Nagarajan, V.1    Thompson, L.D.2
  • 40
    • 0021316249 scopus 로고
    • Bacillus subtilis secretion vector system derived from the B. subtilis α-amylase promoter and signal sequence region and secretion of Escherichia coli β-lactamase by the vector system
    • Ohmura, K.; Shiroza, T.; Nakamura, K.; Nakayama, A.; Yamane, K.; Yoda, K.; Yamasaki, M.; Tamura, G. A. Bacillus subtilis secretion vector system derived from the B. subtilis α-amylase promoter and signal sequence region and secretion of Escherichia coli β-lactamase by the vector system. J. Biochem. 1984, 95, 87-93.
    • (1984) J. Biochem. , vol.95 , pp. 87-93
    • Ohmura, K.1    Shiroza, T.2    Nakamura, K.3    Nakayama, A.4    Yamane, K.5    Yoda, K.6    Yamasaki, M.7    Tamura, G.A.8
  • 41
    • 0023049253 scopus 로고
    • Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation
    • Orii, Y.; Webster, D. A. Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation. J. Biol. Chem. 1986, 261, 3544-3547.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3544-3547
    • Orii, Y.1    Webster, D.A.2
  • 42
    • 0028171092 scopus 로고
    • Effect of Vitreoscilla hemoglobin expression on growth an specific tissue plasminogen activator productivity in recombinant Chinese hamster ovary cells
    • Pendse, G. J.; Bailey, J. E. Effect of Vitreoscilla hemoglobin expression on growth an specific tissue plasminogen activator productivity in recombinant Chinese hamster ovary cells. Biotechnol. Bioeng. 1994, 44, 1367-1370.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1367-1370
    • Pendse, G.J.1    Bailey, J.E.2
  • 43
    • 0017652017 scopus 로고
    • Extracellular enzyme synthesis in genus Bacillus
    • Priest, F. G. Extracellular enzyme synthesis in genus Bacillus. Bacteriol. Rev. 1977, 41, 711-735.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 711-735
    • Priest, F.G.1
  • 46
    • 0001304997 scopus 로고
    • Expression of Vitreoscilla hemoglobin in Corynebacterium glutamicum increases final concentration and yield of L-lysine
    • Alberghina, L., Frontali, L., Sensi P., Eds.; Elsevier Science B. V.: Amsterdam
    • Sander, F. C.; Fachini, R. A.; Hughes, D. E.; Galazzo, J. L.; Bailey, J. E. Expression of Vitreoscilla hemoglobin in Corynebacterium glutamicum increases final concentration and yield of L-lysine. In Progress in Biotechnology. ECB6:Proceedings of the 6th European Congress on Biotechnology; Alberghina, L., Frontali, L., Sensi P., Eds.; Elsevier Science B. V.: Amsterdam, 1994; Vol. 6, pp 607-610.
    • (1994) Progress in Biotechnology. ECB6:Proceedings of the 6th European Congress on Biotechnology , vol.6 , pp. 607-610
    • Sander, F.C.1    Fachini, R.A.2    Hughes, D.E.3    Galazzo, J.L.4    Bailey, J.E.5
  • 48
    • 0025864538 scopus 로고
    • Secretion from B. subtilis of a 34 amino acid residue fragment of human parathyroid hormone: Effect of sequences adjacent to the signal sequence cleavage
    • Saunders, C. W.; Pedroni, J. A.; Monahan, P. Secretion from B. subtilis of a 34 amino acid residue fragment of human parathyroid hormone: effect of sequences adjacent to the signal sequence cleavage. Gene 1991, 102, 277-282.
    • (1991) Gene , vol.102 , pp. 277-282
    • Saunders, C.W.1    Pedroni, J.A.2    Monahan, P.3
  • 50
    • 0023009067 scopus 로고
    • Secretion of mature IFN-α2 and accumulation of uncleaved precursor by Bacillus subtilis transformed with a hybrid α-amylase signal sequence-IFN-α2 gene
    • Schein, C. H.; Kashiwagi, K.; Fujisawa, A.; Weissman, C. Secretion of mature IFN-α2 and accumulation of uncleaved precursor by Bacillus subtilis transformed with a hybrid α-amylase signal sequence-IFN-α2 gene. Bio/Technology 1986, 4, 719-725.
    • (1986) Bio/Technology , vol.4 , pp. 719-725
    • Schein, C.H.1    Kashiwagi, K.2    Fujisawa, A.3    Weissman, C.4
  • 51
    • 0023287630 scopus 로고
    • Optimal gene expression and amplification strategies for batch and continuous recombinant cultures
    • Seressiotis, A.; Bailey, J. E. Optimal gene expression and amplification strategies for batch and continuous recombinant cultures. Biotechnol. Bioeng. 1987, 29, 392-398.
    • (1987) Biotechnol. Bioeng. , vol.29 , pp. 392-398
    • Seressiotis, A.1    Bailey, J.E.2
  • 52
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen, M.; Palva, I. Protein secretion in Bacillus species. Microbiol. Rev. 1993, 57, 109-137.
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 53
    • 0002625568 scopus 로고
    • Regulatory proteins that control late-growth development
    • Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC
    • Smith, I. Regulatory proteins that control late-growth development. In Bacillus subtilis and other gram-positive bacteria; Sonnenshein, A. L., Hoch, J. A., Losick, R., Eds.; American Society for Microbiology: Washington, DC, 1993; pp 785-800.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 785-800
    • Smith, I.1
  • 57
    • 0016192420 scopus 로고
    • Reduced nicotinaminde adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla
    • Webster, D. A.; Liu, C. Y. Reduced nicotinaminde adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. J. Biol. Chem. 1974, 249, 4257-4260.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4257-4260
    • Webster, D.A.1    Liu, C.Y.2
  • 58
    • 0001089022 scopus 로고
    • Western blotting
    • Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., Strahl, K., Eds.; John Wiley & Sons, Inc.: New York
    • Winston, S. E.; Fuller, S. A.; Hurrell, J. G. R. Western blotting. In Current protocols in molecular biology; Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., Strahl, K., Eds.; John Wiley & Sons, Inc.: New York, 1987; pp 10.8.1-10.8.6.
    • (1987) Current Protocols in Molecular Biology
    • Winston, S.E.1    Fuller, S.A.2    Hurrell, J.G.R.3
  • 59
    • 0022848673 scopus 로고
    • Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis
    • Wong, S.-L.; Doi, R. H. Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis. J. Biol. Chem. 1986, 261, 10176-10181.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10176-10181
    • Wong, S.-L.1    Doi, R.H.2
  • 60
    • 0002412951 scopus 로고
    • Use of Escherichia coli lac repressor and operator to control gene expression in Bacillus subtilis
    • Yansura, D. G.; Henner, D. J. Use of Escherichia coli lac repressor and operator to control gene expression in Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 1984, 81, 439-443.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 439-443
    • Yansura, D.G.1    Henner, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.