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Volumn 9, Issue 4, 1999, Pages 365-372

N-Glycosylation of a mouse IgG expressed in transgenic tobacco plants

Author keywords

Monoclonal antibody; N glycosylation; Transgenic plants

Indexed keywords

GLYCAN; GLYCOPROTEIN; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; OLIGOSACCHARIDE; RECOMBINANT PROTEIN;

EID: 0032931237     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.4.365     Document Type: Article
Times cited : (180)

References (30)
  • 1
    • 0026027466 scopus 로고
    • Rapid characterization of asparagine-linked oligosaccharides isolated from glycoproteins using a carbohydrate analyser
    • Anumula, K.R. and Taylor, P.B. (1991) Rapid characterization of asparagine-linked oligosaccharides isolated from glycoproteins using a carbohydrate analyser. Eur. J. Biochem., 195, 269-280.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 269-280
    • Anumula, K.R.1    Taylor, P.B.2
  • 2
    • 0025477259 scopus 로고
    • Synthesis and self-assembly of a functional monoclonal antibody in transgenic Nicotiana tabacum
    • During, K., Hippe, S., Kreuzaler, F. and Schell, J. (1990) Synthesis and self-assembly of a functional monoclonal antibody in transgenic Nicotiana tabacum. Plant Mol. Biol., 15, 281-293.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 281-293
    • During, K.1    Hippe, S.2    Kreuzaler, F.3    Schell, J.4
  • 3
    • 0022186574 scopus 로고
    • Characterization of N-linked oligosaccharides by affinoblotting with concanavalin A-peroxidase and treatment of the blots with glycosidases
    • Faye, L. and Chrispeels, M.J. (1985) Characterization of N-linked oligosaccharides by affinoblotting with concanavalin A-peroxidase and treatment of the blots with glycosidases. Anal. Biochem., 149, 218-224.
    • (1985) Anal. Biochem. , vol.149 , pp. 218-224
    • Faye, L.1    Chrispeels, M.J.2
  • 4
    • 0027453187 scopus 로고
    • Affinity purification of antibodies specific for Asn-linked glycans containing α 1-3 fucose or β 1-2 xylose
    • Faye, L., Gomord, V., Fitchette-Lainé, A-C. and Chrispeels, M.J. (1993) Affinity purification of antibodies specific for Asn-linked glycans containing α 1-3 fucose or β 1-2 xylose. Anal. Biochem., 109, 104-108.
    • (1993) Anal. Biochem. , vol.109 , pp. 104-108
    • Faye, L.1    Gomord, V.2    Fitchette-Lainé, A.-C.3    Chrispeels, M.J.4
  • 7
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T. and Ikenaka, T. (1984) Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem., 95, 197-203.
    • (1984) J. Biochem. , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 8
    • 0024851872 scopus 로고
    • Monosaccharide analysis of glycoconjugates by high-performance anion-exchange chromatography with pulsed amperometric detection
    • Hardy, M.R. (1989) Monosaccharide analysis of glycoconjugates by high-performance anion-exchange chromatography with pulsed amperometric detection. Methods Enzymol., 179, 76-82.
    • (1989) Methods Enzymol. , vol.179 , pp. 76-82
    • Hardy, M.R.1
  • 9
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A.C., Cafferkey, R. and Bowdish, K. (1989) Production of antibodies in transgenic plants. Nature, 342, 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.C.1    Cafferkey, R.2    Bowdish, K.3
  • 10
    • 0031015976 scopus 로고    scopus 로고
    • Glycosylation of antibody molecules: Structural and functional significance
    • Jefferis, R. and Lund, J. (1997) Glycosylation of antibody molecules: structural and functional significance. Antibody Eng. Chem. Immnnol., 65, 111-128.
    • (1997) Antibody Eng. Chem. Immnnol. , vol.65 , pp. 111-128
    • Jefferis, R.1    Lund, J.2
  • 12
    • 0029411968 scopus 로고
    • Immunotherapeutic potential of antibodies produced in plants
    • Ma, J.K.-C. and Hein, M.B. (1995) Immunotherapeutic potential of antibodies produced in plants. Trends Biotechnol., 13, 522-527.
    • (1995) Trends Biotechnol. , vol.13 , pp. 522-527
    • Ma, J.K.-C.1    Hein, M.B.2
  • 13
    • 0025005593 scopus 로고
    • An investigation into the mechanism of protection by local passive immunisation with monoclonal antibodies against Streptococcus mutans
    • Ma, J.K.-C., Hunjan, M., Smith, R. Kelly, C. and Lehner, T. (1990) An investigation into the mechanism of protection by local passive immunisation with monoclonal antibodies against Streptococcus mutans. Infect Immunol., 58, 3407-3414.
    • (1990) Infect Immunol. , vol.58 , pp. 3407-3414
    • Ma, J.K.-C.1    Hunjan, M.2    Smith, R.3    Kelly, C.4    Lehner, T.5
  • 14
    • 0028031827 scopus 로고
    • Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants
    • Ma, J.K.-C., Lehner, T., Stabila, P., Fux, C.I. and Hiatt, A. (1994) Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants. Eur. J. Immunol., 24, 131-138.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 131-138
    • Ma, J.K.-C.1    Lehner, T.2    Stabila, P.3    Fux, C.I.4    Hiatt, A.5
  • 16
    • 0031590175 scopus 로고    scopus 로고
    • a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.)
    • a carbohydrate motif in a secretory peroxidase from a plant cell suspension culture (Vaccinium myrtillus L.). FEBS Lett., 415, 186-191.
    • (1997) FEBS Lett. , vol.415 , pp. 186-191
    • Melo, N.S.1    Nimtz, M.2    Conradt, H.3    Fevereiro, P.S.4    Costa, J.5
  • 17
    • 0023414234 scopus 로고
    • Structure of the sugar chains of mouse immunoglobulin G
    • Mizuochi, T., Hamako, J. and Titani, K. (1987) Structure of the sugar chains of mouse immunoglobulin G. Arch. Biochem. Biophys., 257, 387-394.
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 387-394
    • Mizuochi, T.1    Hamako, J.2    Titani, K.3
  • 18
    • 0029024988 scopus 로고
    • Exploring transgenic plants as a new vaccine source
    • Moffat, A.S. (1995) Exploring transgenic plants as a new vaccine source. Science, 268, 658-660.
    • (1995) Science , vol.268 , pp. 658-660
    • Moffat, A.S.1
  • 23
    • 0030038134 scopus 로고    scopus 로고
    • N-Glycosylation of phytohemagglutinin expressed in bean cotyledons or in transgenic tobacco plants
    • Rayon, C., Gomord, V., Faye, L. and Lerouge, P. (1996) N-Glycosylation of phytohemagglutinin expressed in bean cotyledons or in transgenic tobacco plants. Plant Physiol. Biochem., 34, 273-281.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 273-281
    • Rayon, C.1    Gomord, V.2    Faye, L.3    Lerouge, P.4
  • 25
    • 0024508462 scopus 로고
    • Clonal analysis of the glycosylation of immunoglobulin G secreted by murine hybridomas
    • Rothman, R.J., Warren, L., Vliegenthart, J.F.G. and Hard, K.J. (1989) Clonal analysis of the glycosylation of immunoglobulin G secreted by murine hybridomas. Biochemistry, 28, 1377-1384.
    • (1989) Biochemistry , vol.28 , pp. 1377-1384
    • Rothman, R.J.1    Warren, L.2    Vliegenthart, J.F.G.3    Hard, K.J.4
  • 26
    • 0024728961 scopus 로고
    • Characterisation of monoclonal antibodies to common protein epitopes on the cell surface of Streptococcus sobrinus
    • Smith, R. and Lehner, T. (1989) Characterisation of monoclonal antibodies to common protein epitopes on the cell surface of Streptococcus sobrinus. Oral Microbiol. Immunol., 4, 153-158.
    • (1989) Oral Microbiol. Immunol. , vol.4 , pp. 153-158
    • Smith, R.1    Lehner, T.2
  • 27
    • 0023092177 scopus 로고
    • Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G
    • Takahashi, N., Ishii, I., Ishihara, H., Mori, M., Tejima, S., Jefferis, R., Endo, S. and Arata, Y. (1987) Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G. Biochemistry, 26, 1137-1144.
    • (1987) Biochemistry , vol.26 , pp. 1137-1144
    • Takahashi, N.1    Ishii, I.2    Ishihara, H.3    Mori, M.4    Tejima, S.5    Jefferis, R.6    Endo, S.7    Arata, Y.8
  • 28
    • 0023353924 scopus 로고
    • Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography
    • Tomiya, N., Kurono, M., Ishihara, H., Tejima, S., Endo, S., Arata, Y. and Takahashi, N. (1987) Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography. Anal. Biochem., 163, 489-499.
    • (1987) Anal. Biochem. , vol.163 , pp. 489-499
    • Tomiya, N.1    Kurono, M.2    Ishihara, H.3    Tejima, S.4    Endo, S.5    Arata, Y.6    Takahashi, N.7
  • 29
    • 0023948708 scopus 로고
    • Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
    • Tomiya, N., Awaya, J., Kurono, M., Endo, S., Arata, Y. and Takahashi, N. (1988) Analyses of N-linked oligosaccharides using a two-dimensional mapping technique. Anal. Biochem., 171, 73-90.
    • (1988) Anal. Biochem. , vol.171 , pp. 73-90
    • Tomiya, N.1    Awaya, J.2    Kurono, M.3    Endo, S.4    Arata, Y.5    Takahashi, N.6
  • 30
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • Wright, A. and Morrison, S.L. (1997) Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotechnol., 15, 26-32.
    • (1997) Trends Biotechnol. , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.