메뉴 건너뛰기




Volumn 47, Issue 1, 2006, Pages 144-151

Efficient solubilization, activation, and purification of recombinant Cry45Aa of Bacillus thuringiensis expressed as inclusion bodies in Escherichia coli

Author keywords

CACO 2 cells; Cry protein; Cytotoxic activity; Delta endotoxin; Parasporin

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL TOXIN; ENDOTOXIN; HEMOLYSIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; PARASPORIN; RECOMBINANT PROTEIN;

EID: 33646105851     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.10.011     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 3042697333 scopus 로고    scopus 로고
    • Bacillus thuringiensis serovar shandongiensis strain 89-T-34-22 produces multiple cytotoxic proteins with similar molecular masses against human cancer cells
    • Okumura S., Akao T., Higuchi K., Saitoh H., Mizuki E., Ohba M., and Inouye K. Bacillus thuringiensis serovar shandongiensis strain 89-T-34-22 produces multiple cytotoxic proteins with similar molecular masses against human cancer cells. Lett. Appl. Microbiol. 39 (2004) 89-92
    • (2004) Lett. Appl. Microbiol. , vol.39 , pp. 89-92
    • Okumura, S.1    Akao, T.2    Higuchi, K.3    Saitoh, H.4    Mizuki, E.5    Ohba, M.6    Inouye, K.7
  • 2
    • 0034720456 scopus 로고    scopus 로고
    • Noninsecticidal parasporal proteins of a Bacillus thuringiensis serovar shandongiensis isolate exhibit a preferential cytotoxicity against human leukemic T cells
    • Lee D.-W., Akao T., Yamashita S., Katayama H., Maeda M., Saitoh H., Mizuki E., and Ohba M. Noninsecticidal parasporal proteins of a Bacillus thuringiensis serovar shandongiensis isolate exhibit a preferential cytotoxicity against human leukemic T cells. Biochem. Biophys. Res. Commun. 272 (2000) 218-223
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 218-223
    • Lee, D.-W.1    Akao, T.2    Yamashita, S.3    Katayama, H.4    Maeda, M.5    Saitoh, H.6    Mizuki, E.7    Ohba, M.8
  • 3
    • 23844486577 scopus 로고    scopus 로고
    • Identification of a novel cytotoxic protein, Cry45Aa, from Bacillus thuringiensis A1470 and its selective cytotoxic activity against various mammalian cell lines
    • Okumura S., Saitoh H., Ishikawa T., Wasano N., Yamashita S., Kusumoto K., Akao T., Mizuki E., Ohba M., and Inouye K. Identification of a novel cytotoxic protein, Cry45Aa, from Bacillus thuringiensis A1470 and its selective cytotoxic activity against various mammalian cell lines. J. Agric. Food Chem. 53 (2005) 6313-6318
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 6313-6318
    • Okumura, S.1    Saitoh, H.2    Ishikawa, T.3    Wasano, N.4    Yamashita, S.5    Kusumoto, K.6    Akao, T.7    Mizuki, E.8    Ohba, M.9    Inouye, K.10
  • 4
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Höfte H., and Whiteley H.R. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53 (1989) 242-255
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 5
    • 0027011749 scopus 로고
    • History of Bacillus thuringiensis Berliner research and development
    • Beegle C.C., and Yamamoto T. History of Bacillus thuringiensis Berliner research and development. Can. Entomol. 124 (1992) 587-616
    • (1992) Can. Entomol. , vol.124 , pp. 587-616
    • Beegle, C.C.1    Yamamoto, T.2
  • 7
    • 0026596692 scopus 로고
    • Distribution, frequency, and diversity of Bacillus thuringiensis in an animal feed mill
    • Meadows M.P., Ellis D.J., Butt J., Jarrett P., and Burges H.D. Distribution, frequency, and diversity of Bacillus thuringiensis in an animal feed mill. Appl. Environ. Microbiol. 58 (1992) 1344-1350
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1344-1350
    • Meadows, M.P.1    Ellis, D.J.2    Butt, J.3    Jarrett, P.4    Burges, H.D.5
  • 8
    • 0029667011 scopus 로고    scopus 로고
    • Bacillus thuringiensis populations naturally occurring on mulberry leaves: a possible source of the populations associated with silkworm-rearing insectaries
    • Ohba M. Bacillus thuringiensis populations naturally occurring on mulberry leaves: a possible source of the populations associated with silkworm-rearing insectaries. J. Appl. Microbiol. 80 (1996) 56-64
    • (1996) J. Appl. Microbiol. , vol.80 , pp. 56-64
    • Ohba, M.1
  • 9
    • 0035952344 scopus 로고    scopus 로고
    • Screening of the Bacillus thuringiensis Cry1Ac delta-endotoxin on the artificial phospholipid monolayer incorporated with brush border membrane vesicles of Plutella xylostella by optical biosensor technology
    • Okumura S., Akao T., Mizuki E., Ohba M., and Inouye K. Screening of the Bacillus thuringiensis Cry1Ac delta-endotoxin on the artificial phospholipid monolayer incorporated with brush border membrane vesicles of Plutella xylostella by optical biosensor technology. J. Biochem. Biophys. Methods 47 (2001) 177-188
    • (2001) J. Biochem. Biophys. Methods , vol.47 , pp. 177-188
    • Okumura, S.1    Akao, T.2    Mizuki, E.3    Ohba, M.4    Inouye, K.5
  • 10
    • 0033032037 scopus 로고    scopus 로고
    • Unique activity associated with non-insecticidal Bacillus thuringiensis parasporal inclusions: in vitro cell-killing action on human cancer cells
    • Mizuki E., Ohba M., Akao T., Yamashita S., Saitoh H., and Park Y.S. Unique activity associated with non-insecticidal Bacillus thuringiensis parasporal inclusions: in vitro cell-killing action on human cancer cells. J. Appl. Microbiol. 86 (1999) 477-486
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 477-486
    • Mizuki, E.1    Ohba, M.2    Akao, T.3    Yamashita, S.4    Saitoh, H.5    Park, Y.S.6
  • 13
    • 0033853434 scopus 로고    scopus 로고
    • In vitro cytotoxicity of non-cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells
    • Kim H.-S., Yamashita S., Akao T., Saitoh H., Higuchi K., Park Y.S., Mizuki E., and Ohba M. In vitro cytotoxicity of non-cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells. J. Appl. Microbiol. 89 (2000) 16-23
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 16-23
    • Kim, H.-S.1    Yamashita, S.2    Akao, T.3    Saitoh, H.4    Higuchi, K.5    Park, Y.S.6    Mizuki, E.7    Ohba, M.8
  • 14
    • 0043207521 scopus 로고    scopus 로고
    • Cloning and characterization of two novel crystal protein genes from a Bacillus thuringiensis serovar dakota strain
    • Kim H.-S., Saitoh H., Yamashita S., Akao T., Park Y.S., Maeda M., Tanaka R., Mizuki E., and Ohba M. Cloning and characterization of two novel crystal protein genes from a Bacillus thuringiensis serovar dakota strain. Curr. Microbiol. 46 (2003) 33-38
    • (2003) Curr. Microbiol. , vol.46 , pp. 33-38
    • Kim, H.-S.1    Saitoh, H.2    Yamashita, S.3    Akao, T.4    Park, Y.S.5    Maeda, M.6    Tanaka, R.7    Mizuki, E.8    Ohba, M.9
  • 16
    • 17044401845 scopus 로고    scopus 로고
    • Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis
    • Katayama H., Yokota H., Akao T., Nakamura O., Ohba M., Mekada E., and Mizuki E. Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. J. Biochem. (Tokyo) 137 (2005) 17-25
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 17-25
    • Katayama, H.1    Yokota, H.2    Akao, T.3    Nakamura, O.4    Ohba, M.5    Mekada, E.6    Mizuki, E.7
  • 17
    • 0026684615 scopus 로고
    • Characterization of the pH-mediated solubility of Bacillus thuringiensis var. san diego native delta-endotoxin crystals
    • Koller C.N., Bauer L.S., and Hollingworth R.M. Characterization of the pH-mediated solubility of Bacillus thuringiensis var. san diego native delta-endotoxin crystals. Biochem. Biophys. Res. Commun. 184 (1992) 692-699
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 692-699
    • Koller, C.N.1    Bauer, L.S.2    Hollingworth, R.M.3
  • 18
    • 11944271430 scopus 로고
    • Solubility as a function of protein structure and solvent components
    • Schein C.H. Solubility as a function of protein structure and solvent components. Biotechnology 8 (1990) 308-317
    • (1990) Biotechnology , vol.8 , pp. 308-317
    • Schein, C.H.1
  • 19
    • 0032731203 scopus 로고    scopus 로고
    • Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli
    • Oneda H., and Inouye K. Refolding and recovery of recombinant human matrix metalloproteinase 7 (matrilysin) from inclusion bodies expressed by Escherichia coli. J. Biochem. (Tokyo) 126 (1999) 905-911
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 905-911
    • Oneda, H.1    Inouye, K.2
  • 20
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10 (2000) 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 21
    • 0031950560 scopus 로고    scopus 로고
    • Refolding of recombinant proteins
    • Clark E.D.B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9 (1998) 157-163
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 157-163
    • Clark, E.D.B.1
  • 22
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P. Preparative protein refolding. Trends. Biotechnol. 20 (2002) 437-443
    • (2002) Trends. Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.P.1
  • 23
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg M.E., Rudolph R., and Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30 (1991) 2790-2797
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 24
    • 0030251904 scopus 로고    scopus 로고
    • The specificity of protein aggregation
    • Yon J.M. The specificity of protein aggregation. Nat. Biotechnol. 14 (1996) 1231
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1231
    • Yon, J.M.1
  • 25
    • 2642583349 scopus 로고    scopus 로고
    • Optimised expression in Escherichia coli and purification of the functional form of the Bacillus thuringiensis Cry4Aa delta-endotoxin
    • Boonserm P., Pornwiroon W., Katzenmeier G., Panyim S., and Angsuthanasombat C. Optimised expression in Escherichia coli and purification of the functional form of the Bacillus thuringiensis Cry4Aa delta-endotoxin. Protein Expr. Purif. 35 (2004) 397-403
    • (2004) Protein Expr. Purif. , vol.35 , pp. 397-403
    • Boonserm, P.1    Pornwiroon, W.2    Katzenmeier, G.3    Panyim, S.4    Angsuthanasombat, C.5
  • 28
    • 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. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0030828430 scopus 로고    scopus 로고
    • Cytotoxic effect of immunoconjugate composed of glucose-oxidase coupled to an anti-ganglioside (GD2) antibody on spheroids
    • Heiss P., Bernatz S., Bruchelt G., and Senekowitsch-Schmidtke R. Cytotoxic effect of immunoconjugate composed of glucose-oxidase coupled to an anti-ganglioside (GD2) antibody on spheroids. Anticancer Res. 17 (1997) 3177-3178
    • (1997) Anticancer Res. , vol.17 , pp. 3177-3178
    • Heiss, P.1    Bernatz, S.2    Bruchelt, G.3    Senekowitsch-Schmidtke, R.4
  • 31
    • 33645378416 scopus 로고
    • A nomographic probit solution for the median effective dose (ED50)
    • Koch W., and Kaplan D. A nomographic probit solution for the median effective dose (ED50). J. Immunol. 65 (1950) 7-16
    • (1950) J. Immunol. , vol.65 , pp. 7-16
    • Koch, W.1    Kaplan, D.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 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0023849688 scopus 로고
    • Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments
    • Yin H.L., Iida K., and Janmey P.A. Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J. Cell Biol. 106 (1988) 805-812
    • (1988) J. Cell Biol. , vol.106 , pp. 805-812
    • Yin, H.L.1    Iida, K.2    Janmey, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.