메뉴 건너뛰기




Volumn 40, Issue 6, 2007, Pages 875-880

Cloning and characterization of a single chain antibody to glucose oxidase from a murine hybridoma

Author keywords

Bacterial expression; Glucose oxidase; Monoclonal antibody; Single chain antibody

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MURINAE;

EID: 36949007614     PISSN: 12258687     EISSN: 02191024     Source Type: Journal    
DOI: 10.5483/bmbrep.2007.40.6.875     Document Type: Article
Times cited : (6)

References (38)
  • 2
    • 10644262152 scopus 로고    scopus 로고
    • Isolation and characterization of the human monoclonal antibodies C10 in single-chain fragment variable (scFv) format to glucose oxidase from Aspergillus niger
    • Ascione, A., Flego, M., Zamboni, S., De Cinti, E., Dupuis, M. L. and Cianfriglia, M. (2004) Isolation and characterization of the human monoclonal antibodies C10 in single-chain fragment variable (scFv) format to glucose oxidase from Aspergillus niger. Hybrid. Hybridomics 23, 380-384.
    • (2004) Hybrid. Hybridomics , vol.23 , pp. 380-384
    • Ascione, A.1    Flego, M.2    Zamboni, S.3    De Cinti, E.4    Dupuis, M.L.5    Cianfriglia, M.6
  • 3
    • 0037398639 scopus 로고    scopus 로고
    • The effect of dilution on the rate of hydrogen peroxide production in honey and its implications for wound healing
    • Bang, L. M., Buntting, C. and Molan, P. (2003) The effect of dilution on the rate of hydrogen peroxide production in honey and its implications for wound healing. J. Altern. Complement. Med. 9, 267-273.
    • (2003) J. Altern. Complement. Med , vol.9 , pp. 267-273
    • Bang, L.M.1    Buntting, C.2    Molan, P.3
  • 4
    • 0026526361 scopus 로고
    • Bispecific IgA/IgM antibodies and their use in enzyme immunoassay
    • Behrsing, O., Kaiser, G., Karawajew, L. and Micheel, B. (1992) Bispecific IgA/IgM antibodies and their use in enzyme immunoassay. J. Immunol. Meth. 156, 69-77.
    • (1992) J. Immunol. Meth , vol.156 , pp. 69-77
    • Behrsing, O.1    Kaiser, G.2    Karawajew, L.3    Micheel, B.4
  • 5
    • 0034858966 scopus 로고    scopus 로고
    • Biological sequences integrated: A relational database approach
    • Bergholz, A., Heymann, S., Schenk, J. A. and Freytag, J. C. (2001) Biological sequences integrated: a relational database approach. Acta Biotheor. 49, 145-159.
    • (2001) Acta Biotheor , vol.49 , pp. 145-159
    • Bergholz, A.1    Heymann, S.2    Schenk, J.A.3    Freytag, J.C.4
  • 7
    • 0025151612 scopus 로고
    • Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding
    • Bhat, T. N., Bentley, G. A., Fischmann, T. O., Boulot, G. and Poljak, R. J. (1990) Small rearrangements in structures of Fv and Fab fragments of antibody D1.3 on antigen binding. Nature 347, 483-485.
    • (1990) Nature , vol.347 , pp. 483-485
    • Bhat, T.N.1    Bentley, G.A.2    Fischmann, T.O.3    Boulot, G.4    Poljak, R.J.5
  • 10
    • 0023053369 scopus 로고
    • Carboxy-terminal regions on the surface of tubulin and microtubules. Epitope locations of YOL1/34, DM1A and DM1B
    • Breitling, F. and Little, M. (1986) Carboxy-terminal regions on the surface of tubulin and microtubules. Epitope locations of YOL1/34, DM1A and DM1B. J. Mol. Biol. 189, 367-370.
    • (1986) J. Mol. Biol , vol.189 , pp. 367-370
    • Breitling, F.1    Little, M.2
  • 13
    • 0036366705 scopus 로고    scopus 로고
    • Overview of antibody phage-display technology and its applications
    • Hoogenboom, H. R. (2002) Overview of antibody phage-display technology and its applications. Methods Mol. Biol. 178, 1-37.
    • (2002) Methods Mol. Biol , vol.178 , pp. 1-37
    • Hoogenboom, H.R.1
  • 14
    • 0028889940 scopus 로고
    • Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv)
    • Dübel, S., Breitling, F., Kontermann, R., Schmidt, T., Skerra, A. and Little, M. (1995) Bifunctional and multimeric complexes of streptavidin fused to single chain antibodies (scFv). J. Immunol. Meth. 178, 201-209.
    • (1995) J. Immunol. Meth , vol.178 , pp. 201-209
    • Dübel, S.1    Breitling, F.2    Kontermann, R.3    Schmidt, T.4    Skerra, A.5    Little, M.6
  • 15
    • 0346158535 scopus 로고    scopus 로고
    • Mating antibody phage display with proteomics
    • Hust, M. and Dübel, S. (2004) Mating antibody phage display with proteomics. Trends Biotechnol. 22, 8-14.
    • (2004) Trends Biotechnol , vol.22 , pp. 8-14
    • Hust, M.1    Dübel, S.2
  • 17
    • 1942440453 scopus 로고    scopus 로고
    • Preparation of a highly stable, very active and high-yield multilayered assembly of glucose oxidase using carbohydrate-specific polyclonal antibodies
    • Jan, U. and Husain, Q. (2004) Preparation of a highly stable, very active and high-yield multilayered assembly of glucose oxidase using carbohydrate-specific polyclonal antibodies. Biotechnol. Appl. Biochem. 39, 233-239.
    • (2004) Biotechnol. Appl. Biochem , vol.39 , pp. 233-239
    • Jan, U.1    Husain, Q.2
  • 19
    • 0032965970 scopus 로고    scopus 로고
    • Glucose 1- and 2-oxidases from fungal strains: Isolation and production of monoclonal antibodies
    • Karmali, A. and Oliveira, P. (1999) Glucose 1- and 2-oxidases from fungal strains: isolation and production of monoclonal antibodies. J. Biotechnol. 69, 151-162.
    • (1999) J. Biotechnol , vol.69 , pp. 151-162
    • Karmali, A.1    Oliveira, P.2
  • 20
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G. and Milstein, C. (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256, 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.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
    • 0343415665 scopus 로고    scopus 로고
    • A recombinant bispecific single-chain antibody, CD19 x CD3, induces rapid and high lymphoma-directed cytotoxicity by unstimulated T lymphocytes
    • Loffler, A., Kufer, P., Lutterbuse, R., Zettl, F., Daniel, P. T., Schwenkenbecher, J. M., Riethmuller, G., Dorken, B. and Bargou, R. C. (2000) A recombinant bispecific single-chain antibody, CD19 x CD3, induces rapid and high lymphoma-directed cytotoxicity by unstimulated T lymphocytes. Blood 95, 2098-2103.
    • (2000) Blood , vol.95 , pp. 2098-2103
    • Loffler, A.1    Kufer, P.2    Lutterbuse, R.3    Zettl, F.4    Daniel, P.T.5    Schwenkenbecher, J.M.6    Riethmuller, G.7    Dorken, B.8    Bargou, R.C.9
  • 23
    • 0029993902 scopus 로고    scopus 로고
    • Accessing the Kabat Antibody Sequence Database by Computer
    • Martin, A. C. (1996) Accessing the Kabat Antibody Sequence Database by Computer. Proteins 25, 130-133.
    • (1996) Proteins , vol.25 , pp. 130-133
    • Martin, A.C.1
  • 25
    • 0036678172 scopus 로고    scopus 로고
    • An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells
    • Ng, P. P., Dela Cruz, J. S., Sorour, D. N., Stinebaugh, J. M., Shin, S. U., Shin, D. S., Morrison, S. L. and Penichet, M. L. (2002) An anti-transferrin receptor-avidin fusion protein exhibits both strong proapoptotic activity and the ability to deliver various molecules into cancer cells. Proc. Natl. Acad. Sci. USA 99, 10706-10711.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10706-10711
    • Ng, P.P.1    Dela Cruz, J.S.2    Sorour, D.N.3    Stinebaugh, J.M.4    Shin, S.U.5    Shin, D.S.6    Morrison, S.L.7    Penichet, M.L.8
  • 26
    • 33748911449 scopus 로고    scopus 로고
    • Production and characterization of single chain Fv directed against beta2-agonist clenbuterol
    • Pan, K., Wang, H., Zhang, H. B., Liu, H. W., Lei, H. T., Huang, L. and Sun, Y. M. (2006) Production and characterization of single chain Fv directed against beta2-agonist clenbuterol. J. Agric. Food Chem. 54, 6654-6659.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 6654-6659
    • Pan, K.1    Wang, H.2    Zhang, H.B.3    Liu, H.W.4    Lei, H.T.5    Huang, L.6    Sun, Y.M.7
  • 27
    • 0023724726 scopus 로고
    • Electroporation in biology: Methods, applications, and instrumentation
    • Potter, H. (1988) Electroporation in biology: methods, applications, and instrumentation. Anal. Biochem. 174, 361-373.
    • (1988) Anal. Biochem , vol.174 , pp. 361-373
    • Potter, H.1
  • 28
    • 0023870785 scopus 로고
    • Structure determination of a monoclonal Fab fragment specific for histidine-containing protein of the phosphoenolpyruvate: Sugar phosphotransferase system of Escherichia coli
    • Prasad, L., Vandonselaar, M., Lee, J. S. and Delbaere, L. T. (1988) Structure determination of a monoclonal Fab fragment specific for histidine-containing protein of the phosphoenolpyruvate: sugar phosphotransferase system of Escherichia coli. J. Biol. Chem. 263, 2571-2574.
    • (1988) J. Biol. Chem , vol.263 , pp. 2571-2574
    • Prasad, L.1    Vandonselaar, M.2    Lee, J.S.3    Delbaere, L.T.4
  • 29
    • 0032905950 scopus 로고    scopus 로고
    • Effect of ammonium and nitrate ratio on glucose oxidase activity during gluconic acid fermentation by a mutant strain of Aspergillus niger
    • Ray, S. and Banik, A. K. (1999) Effect of ammonium and nitrate ratio on glucose oxidase activity during gluconic acid fermentation by a mutant strain of Aspergillus niger. Indian J. Exp. Biol. 37, 391-395.
    • (1999) Indian J. Exp. Biol , vol.37 , pp. 391-395
    • Ray, S.1    Banik, A.K.2
  • 31
    • 0028003770 scopus 로고
    • Effects of interleukin 4 on production of IgE monoclonal antibodies directed against glucose oxidase
    • Samoszuk, M. and Yang, Q. B. (1994) Effects of interleukin 4 on production of IgE monoclonal antibodies directed against glucose oxidase. Hybridoma 13, 437-439.
    • (1994) Hybridoma , vol.13 , pp. 437-439
    • Samoszuk, M.1    Yang, Q.B.2
  • 33
    • 6944242577 scopus 로고    scopus 로고
    • Interleukin 4 increases the antibody response against Rubisco in mice
    • Schenk, J. A., Matyssek, F. and Micheel, B. (2004) Interleukin 4 increases the antibody response against Rubisco in mice. In Vivo 18, 649-652.
    • (2004) In Vivo , vol.18 , pp. 649-652
    • Schenk, J.A.1    Matyssek, F.2    Micheel, B.3
  • 34
    • 0034726412 scopus 로고    scopus 로고
    • Schmiedl, A., Breitling, F., Winter, C., Queitsch, I. and Dübel, S. (2000) Effect of engineered Cysteines on yield, solubility and activity in various recombinant antibody formats expressed in E. Coli. J. Immunol. Meth. 242, 101-114.
    • Schmiedl, A., Breitling, F., Winter, C., Queitsch, I. and Dübel, S. (2000) Effect of engineered Cysteines on yield, solubility and activity in various recombinant antibody formats expressed in E. Coli. J. Immunol. Meth. 242, 101-114.
  • 35
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra, A. and Plückthun, A. (1988) Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240, 1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Plückthun, A.2
  • 36
    • 0018775095 scopus 로고
    • Improvement of the glucose oxidase immunoenzyme technic. Use of a tetrazolium whose formazan is stable without heavey metal chelation
    • Suffin, S. C., Muck, K. B., Young, J. C., Lewin, K. and Porter, D. D. (1979) Improvement of the glucose oxidase immunoenzyme technic. Use of a tetrazolium whose formazan is stable without heavey metal chelation. Am. J. Clin. Pathol. 71, 492-496.
    • (1979) Am. J. Clin. Pathol , vol.71 , pp. 492-496
    • Suffin, S.C.1    Muck, K.B.2    Young, J.C.3    Lewin, K.4    Porter, D.D.5
  • 37
    • 1842831044 scopus 로고    scopus 로고
    • Cloning single-chain antibody fragments (scFv) from hybridoma cells
    • Toleikis, L., Broders, O. and Dubel, S. (2004) Cloning single-chain antibody fragments (scFv) from hybridoma cells. Methods Mol. Med. 94, 447-458.
    • (2004) Methods Mol. Med , vol.94 , pp. 447-458
    • Toleikis, L.1    Broders, O.2    Dubel, S.3
  • 38
    • 0033135955 scopus 로고    scopus 로고
    • 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes
    • Wohlfahrt, G., Witt, S., Hendle, J., Schomburg, D., Kalisz, H. M. and Hecht, H. J. (1999) 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallogr. D Biol. Crystallogr. 55, 969-977.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 969-977
    • Wohlfahrt, G.1    Witt, S.2    Hendle, J.3    Schomburg, D.4    Kalisz, H.M.5    Hecht, H.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.