메뉴 건너뛰기




Volumn 67, Issue 6, 2001, Pages 2436-2444

Purification and Characterization of a Psychrophilic, Calcium-Induced, Growth-Phase-Dependent Metalloprotease from the Fish Pathogen Flavobacterium psychrophilum

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; METALLOPROTEINASE;

EID: 0035375081     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.67.6.2436-2444.2001     Document Type: Article
Times cited : (96)

References (55)
  • 1
    • 0023678775 scopus 로고
    • The enzymatic activity of proteinase K is controlled by calcium
    • Bajorath, J., W. Hinrichs, and W. Saenger. 1988. The enzymatic activity of proteinase K is controlled by calcium. Eur. J. Biochem. 176:441-447.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 441-447
    • Bajorath, J.1    Hinrichs, W.2    Saenger, W.3
  • 2
    • 0025196089 scopus 로고
    • 2+-dependent functions in Yersinia pestis
    • 2+-dependent functions in Yersinia pestis. J. Bacteriol. 172:4661-4671.
    • (1990) J. Bacteriol. , vol.172 , pp. 4661-4671
    • Barve, S.S.1    Straley, S.C.2
  • 3
    • 0026022459 scopus 로고
    • Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: Evidence for a regulatory role of LcrH and LcrV
    • Bergman, T., S. Hakansson, A. Forsberg, L. Norlander, A. Macellara, A. Backman, I. Bolin, and H. Wolf-Watz. 1991. Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: evidence for a regulatory role of LcrH and LcrV. J. Bacteriol. 173:1607-1616.
    • (1991) J. Bacteriol. , vol.173 , pp. 1607-1616
    • Bergman, T.1    Hakansson, S.2    Forsberg, A.3    Norlander, L.4    Macellara, A.5    Backman, A.6    Bolin, I.7    Wolf-Watz, H.8
  • 4
    • 0030052649 scopus 로고    scopus 로고
    • Cutting a Gordian knot: Emended classification and description of the genus Flavobacterium, emended description of the family Flavobacteriaceae, and proposal of Flavobacterium hydatis nom. nov.
    • Bernardet, J. F., P. Sergers, M. Vancanneyt, F. Berthe, K. Kersters, and P. Vandamme. 1996. Cutting a Gordian knot: emended classification and description of the genus Flavobacterium, emended description of the family Flavobacteriaceae, and proposal of Flavobacterium hydatis nom. nov. Int. J. Syst. Bacteriol. 46:128-148.
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 128-148
    • Bernardet, J.F.1    Sergers, P.2    Vancanneyt, M.3    Berthe, F.4    Kersters, K.5    Vandamme, P.6
  • 5
    • 0028154647 scopus 로고
    • Electrophorectic detection of proteases from selected strains of Flexibacter psychrophilus and assessment of their variability
    • Bertolini, J. M., H. Wakabayashi, V. G. Watral, M. J. Whipple, and J. S. Rohovec. 1994. Electrophorectic detection of proteases from selected strains of Flexibacter psychrophilus and assessment of their variability. J. Aquat. Anim. Health 6:224-233.
    • (1994) J. Aquat. Anim. Health , vol.6 , pp. 224-233
    • Bertolini, J.M.1    Wakabayashi, H.2    Watral, V.G.3    Whipple, M.J.4    Rohovec, J.S.5
  • 6
    • 0031889267 scopus 로고    scopus 로고
    • A cold-adapted lipase of an Alaskan psychrolroph, Pseudomonas sp. strain B11-1: Gene cloning and enzyme purification and characterization
    • Choo, D.-W., T. Kurihara, T. Suzuki, K. Soda, and N. Esaki. 1998. A cold-adapted lipase of an Alaskan psychrolroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol. 64:486-491.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 486-491
    • Choo, D.-W.1    Kurihara, T.2    Suzuki, T.3    Soda, K.4    Esaki, N.5
  • 7
    • 0031771288 scopus 로고    scopus 로고
    • The Yersinia deadly kiss
    • Cornelis, C. R. 1998. The Yersinia deadly kiss. J. Bacteriol. 180:5495-5504.
    • (1998) J. Bacteriol. , vol.180 , pp. 5495-5504
    • Cornelis, C.R.1
  • 9
    • 0001408577 scopus 로고
    • Virulence mechanisms in Cytophaga psychrophila and other Cytophaga-like bacteria pathogenic for fish
    • Dalsgaard, I. 1993. Virulence mechanisms in Cytophaga psychrophila and other Cytophaga-like bacteria pathogenic for fish. Annu. Rev. Fish Dis. 3:127-144.
    • (1993) Annu. Rev. Fish Dis. , vol.3 , pp. 127-144
    • Dalsgaard, I.1
  • 11
    • 0032802152 scopus 로고    scopus 로고
    • Induction of protease activity in Vibrio anguillarum by gastrointestinal mucus
    • Denkin, S. M., and D. R. Nelson. 1999. Induction of protease activity in Vibrio anguillarum by gastrointestinal mucus. Appl. Environ. Microbiol. 65: 3555-3560.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3555-3560
    • Denkin, S.M.1    Nelson, D.R.2
  • 12
    • 0031973385 scopus 로고    scopus 로고
    • Regulated transcription of Clostridium difficile toxin genes
    • Dupuy, B., and A. L. Sonenshein. 1998. Regulated transcription of Clostridium difficile toxin genes. Mol. Microbiol. 27:107-120.
    • (1998) Mol. Microbiol. , vol.27 , pp. 107-120
    • Dupuy, B.1    Sonenshein, A.L.2
  • 13
    • 0344378199 scopus 로고    scopus 로고
    • Flavobacterium psychrophilum in Baltic salmon Salmo safar brood fish and their offspring
    • Ekman, E., H. Borjeson, and N. Johansson. 1999. Flavobacterium psychrophilum in Baltic salmon Salmo safar brood fish and their offspring. Dis. Aquat. Org. 37:159-163.
    • (1999) Dis. Aquat. Org. , vol.37 , pp. 159-163
    • Ekman, E.1    Borjeson, H.2    Johansson, N.3
  • 14
    • 0034020319 scopus 로고    scopus 로고
    • 2+-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11
    • 2+-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11. Appl. Environ. Microbiol. 66:2021-2028.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2021-2028
    • Exterkate, F.A.1
  • 15
    • 0032962740 scopus 로고    scopus 로고
    • Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase
    • Exterkate, F. A., and A. C. Alting. 1999. Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase. Appl. Environ. Microbiol. 65:1390-1396.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1390-1396
    • Exterkate, F.A.1    Alting, A.C.2
  • 17
    • 0005662543 scopus 로고
    • Columnaris disease: Recent advances in research
    • Griffin, B. R. 1987. Columnaris disease: recent advances in research. Aquaculture 13:48-50.
    • (1987) Aquaculture , vol.13 , pp. 48-50
    • Griffin, B.R.1
  • 18
    • 0025766057 scopus 로고
    • Environmental regulation of bacterial virulence-implication for vaccine design and production
    • Griffiths, E. 1991. Environmental regulation of bacterial virulence-implication for vaccine design and production. Trends Biotechnol. 9:309-315.
    • (1991) Trends Biotechnol. , vol.9 , pp. 309-315
    • Griffiths, E.1
  • 19
    • 0030665692 scopus 로고    scopus 로고
    • Pathogenicity of atypical Aeromonas salmonicida in Atlantic salmon compared with protease production
    • Gunnlaugsdottir, B., and B. K. Gudmundsdottir. 1997. Pathogenicity of atypical Aeromonas salmonicida in Atlantic salmon compared with protease production. J. Appl. Microbiol. 83:543-541.
    • (1997) J. Appl. Microbiol. , vol.83 , pp. 543-1541
    • Gunnlaugsdottir, B.1    Gudmundsdottir, B.K.2
  • 20
    • 0025903435 scopus 로고
    • Genetic basis for virulence in Shigella species
    • Hale, T. L. 1991. Genetic basis for virulence in Shigella species. Microbiol. Rev. 55:206-224.
    • (1991) Microbiol. Rev. , vol.55 , pp. 206-224
    • Hale, T.L.1
  • 21
    • 0038898412 scopus 로고
    • Psychrophiles
    • K. Horikoshi and W. D. Grant (ed.), Wiley, New York, N.Y.
    • Hamamoto, T., and N. J. Russel. 1988. Psychrophiles, p. 1-21. In K. Horikoshi and W. D. Grant (ed.), Extremophiles. Wiley, New York, N.Y.
    • (1988) Extremophiles , pp. 1-21
    • Hamamoto, T.1    Russel, N.J.2
  • 22
    • 0019950356 scopus 로고
    • The influence of glucose, ammonium and magnesium availability on the production of protease and bacitracine by Bacillus licheniformis
    • Haulon, G. H., N. A. Hodges, and A. D. Russell. 1982. The influence of glucose, ammonium and magnesium availability on the production of protease and bacitracine by Bacillus licheniformis. J. Gen. Microbiol. 128:845-851.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 845-851
    • Haulon, G.H.1    Hodges, N.A.2    Russell, A.D.3
  • 23
    • 84985070048 scopus 로고
    • A literature review of the blood chemistry of rainbow trout Salmo gairdneri
    • Hille, S. 1982. A literature review of the blood chemistry of rainbow trout Salmo gairdneri. J. Fish Biol. 20:535-569.
    • (1982) J. Fish Biol. , vol.20 , pp. 535-569
    • Hille, S.1
  • 25
    • 0025238943 scopus 로고
    • The role of the delta-lysin gene (hdl) in the regulation of virulence genes by the accessory gene regulator (agr) in Staphylococcus aureui
    • Janzon, L., and S. Arvidson. 1990. The role of the delta-lysin gene (hdl) in the regulation of virulence genes by the accessory gene regulator (agr) in Staphylococcus aureui. EMBO J. 9:1391-1399.
    • (1990) EMBO J. , vol.9 , pp. 1391-1399
    • Janzon, L.1    Arvidson, S.2
  • 26
    • 0001168188 scopus 로고
    • Effects of photoperiod, temperature and diet on the reconditioning response, blood chemistry and gonad maturation of Atlantic salmon kelts Salmo salar held in freshwater
    • Johnson, C. E., R. W. Gray, A. McLennan, and A. Paterson. 1987. Effects of photoperiod, temperature and diet on the reconditioning response, blood chemistry and gonad maturation of Atlantic salmon kelts Salmo salar held in freshwater. Can. J. Fish. Aquat. Sci. 44:702-711.
    • (1987) Can. J. Fish. Aquat. Sci. , vol.44 , pp. 702-711
    • Johnson, C.E.1    Gray, R.W.2    McLennan, A.3    Paterson, A.4
  • 27
    • 0022405648 scopus 로고
    • Production and partial characterization of an elastolytic protease of Vibrio vulnificus
    • Kothary, M. H., and A. S. Kreger. 1985. Production and partial characterization of an elastolytic protease of Vibrio vulnificus. Infect. Immun. 50:534-540.
    • (1985) Infect. Immun. , vol.50 , pp. 534-540
    • Kothary, M.H.1    Kreger, A.S.2
  • 29
    • 0029879823 scopus 로고
    • A 38 kDa precursor protein of aqualisin I (a thermophilic subtilisin-type protease) with a C-terminal extended sequence: Its precipitation and in vivo processing
    • Kurosaka, K., T. Ohta, and H. Matsuzawa. 1995. A 38 kDa precursor protein of aqualisin I (a thermophilic subtilisin-type protease) with a C-terminal extended sequence: its precipitation and in vivo processing. Mol. Microbiol. 20:385-389.
    • (1995) Mol. Microbiol. , vol.20 , pp. 385-389
    • Kurosaka, K.1    Ohta, T.2    Matsuzawa, H.3
  • 30
    • 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
  • 31
    • 0023693706 scopus 로고
    • Tn5-induced protease-deficient strains of Aeromonas hydrophila with reduced virulence for fish
    • Leung, K. Y., and R. M. W. Stevenson. 1988. Tn5-induced protease-deficient strains of Aeromonas hydrophila with reduced virulence for fish. Infect. Immun. 56:2639-2644.
    • (1988) Infect. Immun. , vol.56 , pp. 2639-2644
    • Leung, K.Y.1    Stevenson, R.M.W.2
  • 32
    • 0014062055 scopus 로고
    • Regulation of extracellular protease production in Bacillus cereus
    • Levishon, S., and A. I. Aronson. 1967. Regulation of extracellular protease production in Bacillus cereus. J. Bacteriol. 93:1023-1030.
    • (1967) J. Bacteriol. , vol.93 , pp. 1023-1030
    • Levishon, S.1    Aronson, A.I.2
  • 33
    • 0000916969 scopus 로고
    • Calcium-dependent pectate lyase production in the soft-rotting bacterium Pseudomonas fluorescens
    • Liao, C.-H., D. E. McCallus, and J. M. Wells. 1993. Calcium-dependent pectate lyase production in the soft-rotting bacterium Pseudomonas fluorescens. Phytopathology 83:813-818.
    • (1993) Phytopathology , vol.83 , pp. 813-818
    • Liao, C.-H.1    McCallus, D.E.2    Wells, J.M.3
  • 34
    • 0031884187 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of an extracellular protease from Pseudomonas fluoresccns CY091
    • Liao, C.-H., and D. E. McCallus. 1998. Biochemical and genetic characterization of an extracellular protease from Pseudomonas fluoresccns CY091. Appl. Environ. Microbiol. 64:914-921.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 914-921
    • Liao, C.-H.1    McCallus, D.E.2
  • 35
    • 0032797930 scopus 로고    scopus 로고
    • Weakly bound calcium ions involved in the thermostability of aqualisin 1, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1
    • Lin, S. J., E. Yoshimura, H. Sakai, T. Wakagi, and H. Matsuzawa. 1999. Weakly bound calcium ions involved in the thermostability of aqualisin 1, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1. Biochim. Biophys. Acta 1433:132-138.
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 132-138
    • Lin, S.J.1    Yoshimura, E.2    Sakai, H.3    Wakagi, T.4    Matsuzawa, H.5
  • 36
    • 0023975368 scopus 로고
    • Purification and partial characterization of a calcium-stimulated protease from the cyanobacterium Anabaena variabilis
    • Lockau, W., B. Massalsky, and A. Dirmeier. 1988. Purification and partial characterization of a calcium-stimulated protease from the cyanobacterium Anabaena variabilis. Eur. J. Biochem. 172:433-438.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 433-438
    • Lockau, W.1    Massalsky, B.2    Dirmeier, A.3
  • 38
    • 0002470618 scopus 로고    scopus 로고
    • Characterization of Flavobacterium psychrophilum; comparison of proteolytic activity and virulence of strains isolated from trout (Oncorhynchus mykiss)
    • A. C. Barnes, G. A. Davidson, M. P. Hiney, and D. McIntosh (ed.), Fisheries Research Service, Aberdeen, Scotland
    • Madsen, L., and I. Dalsgaard. 1998. Characterization of Flavobacterium psychrophilum; comparison of proteolytic activity and virulence of strains isolated from trout (Oncorhynchus mykiss), p. 45-52. In A. C. Barnes, G. A. Davidson, M. P. Hiney, and D. McIntosh (ed.), Methodology in fish disease research. Fisheries Research Service, Aberdeen, Scotland.
    • (1998) Methodology in Fish Disease Research , pp. 45-52
    • Madsen, L.1    Dalsgaard, I.2
  • 39
    • 0026687638 scopus 로고
    • Production and properties of an extracellular metalloprotease from a psychrophilic Pseudomonas fluorescens
    • Margesin, R., and F. Schinner. 1992. Production and properties of an extracellular metalloprotease from a psychrophilic Pseudomonas fluorescens. J. Biotechnol. 24:207-210.
    • (1992) J. Biotechnol. , vol.24 , pp. 207-210
    • Margesin, R.1    Schinner, F.2
  • 40
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group a streptococcus
    • McIver, K. S., and J. R. Scott. 1997. Role of mga in growth phase regulation of virulence genes of the group A streptococcus. J. Bacteriol. 179:5178-5187.
    • (1997) J. Bacteriol. , vol.179 , pp. 5178-5187
    • McIver, K.S.1    Scott, J.R.2
  • 41
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • Mekalanos, J. J. 1992. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 174:1-7.
    • (1992) J. Bacteriol. , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 42
    • 0032705847 scopus 로고    scopus 로고
    • Production of viable cultures of Flavobacterium psychrophilum: Approach and control
    • Michel, C., D. Antonio, and R. P. Hedrick. 1999. Production of viable cultures of Flavobacterium psychrophilum: approach and control. Res. Microbiol. 150:351-358.
    • (1999) Res. Microbiol. , vol.150 , pp. 351-358
    • Michel, C.1    Antonio, D.2    Hedrick, R.P.3
  • 43
    • 0028149818 scopus 로고
    • Regulation of the Yersinia enterocolitica enterotoxin Yst gene: Influence of growth phase, temperature, osmolarity, pH and bacterial host factors
    • Mikulskis, A. V., I. Delor, V. H. Thi, and G. R. Cornelis. 1994. Regulation of the Yersinia enterocolitica enterotoxin Yst gene: influence of growth phase, temperature, osmolarity, pH and bacterial host factors. Mol. Microbiol. 14:905-915.
    • (1994) Mol. Microbiol. , vol.14 , pp. 905-915
    • Mikulskis, A.V.1    Delor, I.2    Thi, V.H.3    Cornelis, G.R.4
  • 44
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP, phoQ) controls Salmonella typhymurium virulence
    • Miller, S. I., A. M. Kukral, and J. J. Mekalanos. 1989. A two-component regulatory system (phoP, phoQ) controls Salmonella typhymurium virulence. Proc. Natl. Acad. Sci. USA 86:5054-5058.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 45
    • 0027234756 scopus 로고
    • Calmodulin-activated bacterial adenylate cyclases as virulence factors
    • Mock, M., and A. Ullmann. 1993. Calmodulin-activated bacterial adenylate cyclases as virulence factors. Trends Microbiol. 1:187-192.
    • (1993) Trends Microbiol. , vol.1 , pp. 187-192
    • Mock, M.1    Ullmann, A.2
  • 46
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase, H., and J. F. Woessner. 1999. Matrix metalloproteinases. J. Biol. Chem. 274:21491-21494.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 47
    • 0026498428 scopus 로고
    • Cloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum
    • Norqvist, A., B. Norrman, and H. Wolf-Watz. 1992. Cloning of a metalloprotease gene involved in the virulence mechanism of Vibrio anguillarum. J. Bacteriol. 174:111-118.
    • (1992) J. Bacteriol. , vol.174 , pp. 111-118
    • Norqvist, A.1    Norrman, B.2    Wolf-Watz, H.3
  • 48
    • 0004290384 scopus 로고
    • Characteristics of myxobacteria isolated from the surface of freshwater fish
    • Pacha, R. E., and S. Porter. 1968. Characteristics of myxobacteria isolated from the surface of freshwater fish. Appl. Microbiol. 16:1901-1906.
    • (1968) Appl. Microbiol. , vol.16 , pp. 1901-1906
    • Pacha, R.E.1    Porter, S.2
  • 49
    • 84988072844 scopus 로고
    • Ultrasensitive silver-based colour staining of polypeptides in polyacrylamide gels
    • Sammons, D. W., L. D. Adams, and E. E. Nishizawa. 1981. Ultrasensitive silver-based colour staining of polypeptides in polyacrylamide gels. Electrophoresis 2:135-140.
    • (1981) Electrophoresis , vol.2 , pp. 135-140
    • Sammons, D.W.1    Adams, L.D.2    Nishizawa, E.E.3
  • 50
    • 0032881907 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular protease from the fish pathogen Yersinia ruckeri and effect of culture conditions on production
    • Secades, P., and J. A. Guijarro. 1999. Purification and characterization of an extracellular protease from the fish pathogen Yersinia ruckeri and effect of culture conditions on production. Appl. Environ. Microbiol. 65:3969-3975.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3969-3975
    • Secades, P.1    Guijarro, J.A.2
  • 51
    • 0031593689 scopus 로고    scopus 로고
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607. Mol. Cell. Biol. 183:183-191.
    • (1998) Mol. Cell. Biol. , vol.183 , pp. 183-191
    • Sharma, S.1    Giri, S.2    Khuller, G.K.3
  • 52
    • 0025998717 scopus 로고
    • Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases
    • Siezen, R. J., W. M. de Vos, J. A. M. Levnissen, and W. Dijkstra. 1991. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4:719-737.
    • (1991) Protein Eng. , vol.4 , pp. 719-737
    • Siezen, R.J.1    De Vos, W.M.2    Levnissen, J.A.M.3    Dijkstra, W.4
  • 53
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W. G., S. Aznavoorian, and L. A. Liotta. 1993. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9:541-573.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 54
    • 0017075046 scopus 로고
    • Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability
    • Voordouw, G., C. Milo, and R. S. Roche. 1976. Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability. Biochemistry 15:3716-3723.
    • (1976) Biochemistry , vol.15 , pp. 3716-3723
    • Voordouw, G.1    Milo, C.2    Roche, R.S.3
  • 55
    • 0023880395 scopus 로고
    • Effects of iron and temperature on Shiga-like toxin I production by Escherichia coli
    • Weinstein, D. L., R. K. Holmes, and A. D. O'Brien. 1988. Effects of iron and temperature on Shiga-like toxin I production by Escherichia coli. Infect. Immun. 56:106-111.
    • (1988) Infect. Immun. , vol.56 , pp. 106-111
    • Weinstein, D.L.1    Holmes, R.K.2    O'Brien, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.