메뉴 건너뛰기




Volumn 64, Issue 1, 1996, Pages 230-237

Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM TOXIN; COLLAGEN; COMPLEMENT COMPONENT C3; FIBRONECTIN; IMMUNOGLOBULIN A; METALLOPROTEINASE; THERMOLYSIN;

EID: 0030058645     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.64.1.230-237.1996     Document Type: Article
Times cited : (66)

References (42)
  • 1
    • 0025457533 scopus 로고
    • Factors involved in the electroporation-induced transformation of Clostridium perfringens
    • Allen, S. P., and H. P. Blaschek. 1990 Factors involved in the electroporation-induced transformation of Clostridium perfringens. FEMS Microbiol Lett 70:217-220.
    • (1990) FEMS Microbiol Lett , vol.70 , pp. 217-220
    • Allen, S.P.1    Blaschek, H.P.2
  • 3
    • 4344680185 scopus 로고
    • Proteolytic enzymes of Clostridium welchu
    • Bidwell, E. 1950 Proteolytic enzymes of Clostridium welchu. Biochem. J. 46:589-598.
    • (1950) Biochem. J. , vol.46 , pp. 589-598
    • Bidwell, E.1
  • 4
    • 0018391216 scopus 로고
    • Influence of iron on yields of extracellular products in Pseudomonas aeruginosa cultures
    • Bjorn, M. J., P. A. Sokol, and B. H. Iglewski. 1979 Influence of iron on yields of extracellular products in Pseudomonas aeruginosa cultures. J. Bacteriol. 138:193-200.
    • (1979) J. Bacteriol. , vol.138 , pp. 193-200
    • Bjorn, M.J.1    Sokol, P.A.2    Iglewski, B.H.3
  • 5
    • 0019376052 scopus 로고
    • Isolation of a plasmid responsible for caseinase activity in Clostridium perfringens ATTC 3626B
    • Blaschek, H. P., and M. Solberg. 1981. Isolation of a plasmid responsible for caseinase activity in Clostridium perfringens ATTC 3626B. J. Bacteriol 147:262-266.
    • (1981) J. Bacteriol , vol.147 , pp. 262-266
    • Blaschek, H.P.1    Solberg, M.2
  • 6
    • 0018074114 scopus 로고
    • Further studies on the mode of action of Clostridium welchu type-D epsilon toxin
    • Buxton, D. 1978. Further studies on the mode of action of Clostridium welchu type-D epsilon toxin J. Med. Microbiol. 11:293-298.
    • (1978) J. Med. Microbiol. , vol.11 , pp. 293-298
    • Buxton, D.1
  • 7
    • 0022965871 scopus 로고
    • Separation of large DNA molecules by contour-clamped homogeneous electric fields
    • Chu, G., D. Vollrath, and R. W. Davis. 1986. Separation of large DNA molecules by contour-clamped homogeneous electric fields. Science 234:1582-1585.
    • (1986) Science , vol.234 , pp. 1582-1585
    • Chu, G.1    Vollrath, D.2    Davis, R.W.3
  • 8
    • 0025644630 scopus 로고
    • Comparison of the Vibrio chalerae hemagglutinin/protease and the Pseudomonas aeruginosa elastase
    • Hase, C. C., and R. A. Finkelstein. 1990. Comparison of the Vibrio chalerae hemagglutinin/protease and the Pseudomonas aeruginosa elastase Infect. Immun. 58:4011-4015.
    • (1990) Infect. Immun. , vol.58 , pp. 4011-4015
    • Hase, C.C.1    Finkelstein, R.A.2
  • 9
    • 0027140429 scopus 로고
    • Bacterial extracellular zinc-containing metalloproteases
    • Häse, C. C., and R. A. Finkelstein. 1993. Bacterial extracellular zinc-containing metalloproteases. Microbiol Rev. 57:823-837
    • (1993) Microbiol Rev. , vol.57 , pp. 823-837
    • Häse, C.C.1    Finkelstein, R.A.2
  • 11
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6 Å resolution
    • Holmes, M. A., and B. W. Matthews. 1982. Structure of thermolysin refined at 1.6 Å resolution. J. Mol. Biol. 160:623-639.
    • (1982) J. Mol. Biol. , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 12
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationships
    • Jiang, W., and J. S. Bond. 1992. Families of metalloendopeptidases and their relationships. FEBS Lett. 312:110-114.
    • (1992) FEBS Lett. , vol.312 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 13
    • 0027535704 scopus 로고
    • Comparison of the alpha-toxin genes of Clostridium perfringens type A and C strains: Evidence for extragenic regulation of transcription
    • Katayama, S.-I., O. Matsushita, J. Minami, S. Mizobuchi, and A. Okabe. 1993. Comparison of the alpha-toxin genes of Clostridium perfringens type A and C strains: evidence for extragenic regulation of transcription. Infect. Immun 61:457-463.
    • (1993) Infect. Immun , vol.61 , pp. 457-463
    • Katayama, S.-I.1    Matsushita, O.2    Minami, J.3    Mizobuchi, S.4    Okabe, A.5
  • 14
    • 0019922452 scopus 로고
    • In vitro inhibition of Pseudomonas aeruginosa elastase by metal-chelating peptide derivatives
    • Kessler, E., M. Israel, N. Landshman, A. Chechick, and S. Blumberg. 1982. In vitro inhibition of Pseudomonas aeruginosa elastase by metal-chelating peptide derivatives. Infect. Immun. 38:716-723.
    • (1982) Infect. Immun. , vol.38 , pp. 716-723
    • Kessler, E.1    Israel, M.2    Landshman, N.3    Chechick, A.4    Blumberg, S.5
  • 15
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • Kumpel, K. R., N. Arora, and S. H. Leppla. 1994. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13:1093-1100.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1093-1100
    • Kumpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 16
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenolypic selection
    • Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenolypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 17
    • 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
  • 18
    • 0017162397 scopus 로고
    • Stable L-forms of Clostridium perfringens and their growth on glass surfaces
    • Mahony, D. E., and T. J. Moore. 1976. Stable L-forms of Clostridium perfringens and their growth on glass surfaces. Can. J Microbiol 22:953-959.
    • (1976) Can. J Microbiol , vol.22 , pp. 953-959
    • Mahony, D.E.1    Moore, T.J.2
  • 19
    • 0028335841 scopus 로고
    • A Clostridium perfringens vector for the selection of promoters
    • Matsushita, C., O. Matsushita, M. Koyama, and A. Okabe. 1994. A Clostridium perfringens vector for the selection of promoters. Plasmid 31:317-319.
    • (1994) Plasmid , vol.31 , pp. 317-319
    • Matsushita, C.1    Matsushita M Koyama, O.2    Okabe, A.3
  • 20
    • 0028084886 scopus 로고
    • Purification and characterization of a Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene
    • Matsushita, O., K. Yoshihara, S.-I. Katayama, J. Minami, and A. Okahe. 1994. Purification and characterization of a Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene J. Bacteriol. 176:149-156.
    • (1994) J. Bacteriol. , vol.176 , pp. 149-156
    • Matsushita, O.1    Yoshihara, K.2    Katayama, S.-I.3    Minami, J.4    Okahe, A.5
  • 22
    • 0026764605 scopus 로고
    • Activation mechanism of human Hageman factor-plasma kallikrein-kinin system by Vibno vidnificus metalloprotease
    • Miyoshi, S.-I., and S. Shinoda. 1992. Activation mechanism of human Hageman factor-plasma kallikrein-kinin system by Vibno vidnificus metalloprotease. FEBS Lett. 308:315-319.
    • (1992) FEBS Lett. , vol.308 , pp. 315-319
    • Miyoshi, S.-I.1    Shinoda, S.2
  • 23
    • 0024340635 scopus 로고
    • Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases
    • Molla, A., T. Yamamoto, T. Akaike, S. Miyoshi, and H. Maeda. 1989 Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases. J. Biol. Chem. 264:10589-10594.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10589-10594
    • Molla, A.1    Yamamoto, T.2    Akaike, T.3    Miyoshi, S.4    Maeda, H.5
  • 24
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulmum neurotoxins
    • Montecucco, C., and G. Schiavo. 1994. Mechanism of action of tetanus and botulmum neurotoxins. Mol. Microbiol. 13:1-8
    • (1994) Mol. Microbiol. , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 25
    • 85063549029 scopus 로고
    • Pseudomonas proteases
    • I. A Holder (ed.), CRC Press, Inc . Boca Raton, Fia
    • Morihara, K., and J. Y. Homma. 1985. Pseudomonas proteases. p. 41-79 In I. A Holder (ed.), Bacterial enzymes and virulence. CRC Press, Inc . Boca Raton, Fia.
    • (1985) Bacterial Enzymes and Virulence , pp. 41-79
    • Morihara, K.1    Homma, J.Y.2
  • 26
    • 0002238821 scopus 로고
    • Pseudomonas metalloproteases and the host-microbe relationship
    • R. B Fick (ed.). CRC Press, Inc.. Boca Raton, Fla
    • Parmely, M. J. 1993. Pseudomonas metalloproteases and the host-microbe relationship, p. 79-94. In R. B Fick (ed.). Pseudomonas aeruginosa the opportunist: pathogenesis and disease. CRC Press, Inc.. Boca Raton, Fla.
    • (1993) Pseudomonas Aeruginosa the Opportunist: Pathogenesis and Disease , pp. 79-94
    • Parmely, M.J.1
  • 27
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 28
    • 0022457635 scopus 로고
    • Modified plasmid isolation method for Clostridium perfringens and Clostridium absonum
    • Roberts, I., W. M. Holmes, and P. B. Hylemon. 1986. Modified plasmid isolation method for Clostridium perfringens and Clostridium absonum. Appl. Environ. Microbiol 52:197-199
    • (1986) Appl. Environ. Microbiol , vol.52 , pp. 197-199
    • Roberts, I.1    Holmes, W.M.2    Hylemon, P.B.3
  • 29
    • 0025824660 scopus 로고
    • Molecular genetics and pathogenesis of Clostridium peifringens
    • Rood, J. I., and S. T. Cole. 1991. Molecular genetics and pathogenesis of Clostridium peifringens. Microbiol. Rev. 55:621-648.
    • (1991) Microbiol. Rev. , vol.55 , pp. 621-648
    • Rood, J.I.1    Cole, S.T.2
  • 30
    • 0023637418 scopus 로고
    • Purification and characterization of Clostridium perfringens beta toxin
    • Sakurai, J., and Y. Fujii. 1987. Purification and characterization of Clostridium perfringens beta toxin. Toxicon 25:1301-1310
    • (1987) Toxicon , vol.25 , pp. 1301-1310
    • Sakurai, J.1    Fujii, Y.2
  • 35
    • 0026689519 scopus 로고
    • Construction of a sequenced Clostridium perfringens-Escherichia coli shuttle plasmid
    • Sloan, J., T. A. Warner, P. T. Scott, T. L. Bannam, D. I. Berryman, and J. I. Rood. 1992. Construction of a sequenced Clostridium perfringens-Escherichia coli shuttle plasmid. Plasmid 27:207-219
    • (1992) Plasmid , vol.27 , pp. 207-219
    • Sloan, J.1    Warner, T.A.2    Scott, P.T.3    Bannam, T.L.4    Berryman, D.I.5    Rood, J.I.6
  • 38
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-Å resolution
    • Thayer, M. M., K. M. Flaherty, and D. B. McKay. 1991. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-Å resolution. J. Biol Chem 266:2864-2871
    • (1991) J. Biol Chem , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 39
    • 0017400132 scopus 로고
    • A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances
    • Weaver, L. H., W. R. Kester, and B. W. Matthews. 1977. A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances. J Mol. Biol. 114:119-132
    • (1977) J Mol. Biol. , vol.114 , pp. 119-132
    • Weaver, L.H.1    Kester, W.R.2    Matthews, B.W.3
  • 40
    • 0028234762 scopus 로고
    • Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F
    • Yamasaki, S., Y. Hu, T. Binz, A. Kalkuhl, H. Kurazono, T. Tamura, R. Jahn, E. Kandel, and H. Niemann. 1994. Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F Proc. Natl. Acad. Sci USA 91:4688-4692.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , pp. 4688-4692
    • Yamasaki, S.1    Hu, Y.2    Binz, T.3    Kalkuhl, A.4    Kurazono, H.5    Tamura, T.6    Jahn, R.7    Kandel, E.8    Niemann, H.9
  • 41
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 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
  • 42
    • 0028075721 scopus 로고
    • Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase
    • Yoshihara, K., O. Matsushita, J. Minami, and A. Okabe. 1994. Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J Bacteriol 176:6489-6496
    • (1994) J Bacteriol , vol.176 , pp. 6489-6496
    • Yoshihara, K.1    Matsushita, O.2    Minami, J.3    Okabe, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.