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Volumn 7, Issue 5, 1997, Pages 635-651

Microheterogeneity of the oligosaccharides carried by the recombinant bovine lactoferrin expressed in Mamestra brassicae cells

Author keywords

Baculovirus vector; Bovine lactoferrin; Insect cell; Mamestra brassicae; N glycosylation

Indexed keywords

LACTOFERRIN; VIRUS VECTOR;

EID: 0030804028     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.5.635     Document Type: Article
Times cited : (40)

References (74)
  • 1
    • 0028909554 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells: Evidence for α-mannosidase II
    • Altmann, F. and März, L. (1995) Processing of asparagine-linked oligosaccharides in insect cells: evidence for α-mannosidase II. Glycoconjugate J., 12, 150-155.
    • (1995) Glycoconjugate J. , vol.12 , pp. 150-155
    • Altmann, F.1    März, L.2
  • 2
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. N-Acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells
    • Altmann, F., Kornfeld, G., Dalik, T., Staudacher, E. and Glössl, J. (1993) Processing of asparagine-linked oligosaccharides in insect cells. N-Acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology, 3, 619-625.
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glössl, J.5
  • 3
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glössl, J. and März, L. (1995) Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem., 270, 17344-17349.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glössl, J.4    März, L.5
  • 4
    • 0027185796 scopus 로고
    • Gene II product of an aphid-nontransmissible isolate of cauliflower mosaic virus expressed in a baculovirus system possesses phid transmission factor activity
    • Blanc, S., Cerutti, M., Chaabihi, H., Louis, C., Devauchelle, G. and Hull, R. (1993) Gene II product of an aphid-nontransmissible isolate of cauliflower mosaic virus expressed in a baculovirus system possesses phid transmission factor activity. Virology, 192, 651-654.
    • (1993) Virology , vol.192 , pp. 651-654
    • Blanc, S.1    Cerutti, M.2    Chaabihi, H.3    Louis, C.4    Devauchelle, G.5    Hull, R.6
  • 5
    • 0025666651 scopus 로고
    • Carbohydrate ligands of the LEC cell adhesion molecules
    • Branley, B.K., Sweidler, S.J. and Robbins, P.W. (1990) Carbohydrate ligands of the LEC cell adhesion molecules. Cell, 63, 861-863.
    • (1990) Cell , vol.63 , pp. 861-863
    • Branley, B.K.1    Sweidler, S.J.2    Robbins, P.W.3
  • 6
    • 0019873857 scopus 로고
    • Isolation and characterization of mosquito cell membrane glycoproteins
    • Butters, T.D. and Hughes, RC. (1981) Isolation and characterization of mosquito cell membrane glycoproteins. Biochim. Biophys. Acta, 640, 655-671.
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 655-671
    • Butters, T.D.1    Hughes, R.C.2
  • 7
    • 0027412448 scopus 로고
    • Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells
    • Chaabihi, H., Ogliastro, M.-H., Martin, M., Giraud, C., Devauchelle, G. and Cerutti, M. (1993) Competition between baculovirus polyhedrin and p10 gene expression during infection of insect cells. J. Virol., 67, 2664-2671.
    • (1993) J. Virol. , vol.67 , pp. 2664-2671
    • Chaabihi, H.1    Ogliastro, M.-H.2    Martin, M.3    Giraud, C.4    Devauchelle, G.5    Cerutti, M.6
  • 8
    • 0025909605 scopus 로고
    • Carbohydrate variant of the recombinant β-subunit of human choriogonadotropin expressed in baculovirus expression system
    • Chen, W., Shen, Q. and Bahl, O.P. (1991) Carbohydrate variant of the recombinant β-subunit of human choriogonadotropin expressed in baculovirus expression system. J. Biol. Chem., 266, 4081-4087.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4081-4087
    • Chen, W.1    Shen, Q.2    Bahl, O.P.3
  • 9
    • 0017773923 scopus 로고
    • Fractionnement chromatographique et études sur la microhétérogénéité de la lactotransferrine de vache préparée par un procédé original
    • Chéron, A., Mazurier, J. and Fournet, B. (1977) Fractionnement chromatographique et études sur la microhétérogénéité de la lactotransferrine de vache préparée par un procédé original. C. R. Acad. Sci. Hebd. Seances Acad. Sci., 284, 585-588.
    • (1977) C. R. Acad. Sci. Hebd. Seances Acad. Sci. , vol.284 , pp. 585-588
    • Chéron, A.1    Mazurier, J.2    Fournet, B.3
  • 10
    • 0027052198 scopus 로고
    • Heterogeneity of bovine lactoferrin glycans. Characterization of α-D-Gal- and α-NeuAc-(2-6)-β-D-GalpNAc-(1-4)-β-D-GlcNAc-substituted N-linked glycans
    • Coddeville, B., Strecker, G., Wieruszeski, J.M., Vliegenthart, J.F.G., Van Halbeek, H., Peter-Katalinic, J., Egge, H. and Spik, G. (1992) Heterogeneity of bovine lactoferrin glycans. Characterization of α-D-Gal- and α-NeuAc-(2-6)-β-D-GalpNAc-(1-4)-β-D-GlcNAc-substituted N-linked glycans. Carbohydr. Res., 236, 145-164.
    • (1992) Carbohydr. Res. , vol.236 , pp. 145-164
    • Coddeville, B.1    Strecker, G.2    Wieruszeski, J.M.3    Vliegenthart, J.F.G.4    Van Halbeek, H.5    Peter-Katalinic, J.6    Egge, H.7    Spik, G.8
  • 11
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • Crestfield, A.M., Moore, S. and Stein, W.H. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem., 238, 622-627.
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 12
    • 0025741695 scopus 로고
    • Structures of the asparagine-289-linked oligosaccharides assembled on recombinant human plasminogen expressed in a Mamestra brassicae cell line (IZD-MBO503)
    • Davidson, D.J. and Castellino, F.J. (1991a) Structures of the asparagine-289-linked oligosaccharides assembled on recombinant human plasminogen expressed in a Mamestra brassicae cell line (IZD-MBO503) Biochemistry, 30, 6689-6696.
    • (1991) Biochemistry , vol.30 , pp. 6689-6696
    • Davidson, D.J.1    Castellino, F.J.2
  • 13
    • 0025773714 scopus 로고
    • Asparagine-linked oligosaccharide processing in lepidopteran insect cells. Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-Sf-21AE) cells
    • Davidson, D.J. and Castellino, F.J. (1991b) Asparagine-linked oligosaccharide processing in lepidopteran insect cells. Temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-Sf-21AE) cells. Biochemistry, 30, 6167-6174.
    • (1991) Biochemistry , vol.30 , pp. 6167-6174
    • Davidson, D.J.1    Castellino, F.J.2
  • 14
    • 0025336176 scopus 로고
    • Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson, D.J., Fraser, M.J. and Castellino, F.J. (1990) Oligosaccharide processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry, 29, 5584-5590.
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.1    Fraser, M.J.2    Castellino, F.J.3
  • 15
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein, A.D. (1987) Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem., 56, 497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 16
    • 0024978864 scopus 로고
    • Cationic liposome-mediated transfection
    • Felgner, P.L. and Ringold, G.M. (1989) Cationic liposome-mediated transfection. Nature, 337, 387-388.
    • (1989) Nature , vol.337 , pp. 387-388
    • Felgner, P.L.1    Ringold, G.M.2
  • 18
    • 0025840338 scopus 로고
    • The oligosaccharides of glycoproteins: Bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties
    • Goochee, C.F., Gramer, M.J., Andersen, D.C., Bahr, J.B. and Rasmussen, J.R. (1991) The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties. Bio/ Technology, 9, 1347-1355.
    • (1991) Bio/ Technology , vol.9 , pp. 1347-1355
    • Goochee, C.F.1    Gramer, M.J.2    Andersen, D.C.3    Bahr, J.B.4    Rasmussen, J.R.5
  • 19
    • 0027296753 scopus 로고
    • Biosynthesis and secretion of human interleukin-2 glycoprotein variants from baculovirus-infected Sf-21 cells
    • Grabenhorst, E., Hofler, B., Nimtz, M., Jager, V. and Conrad, H.S. (1993) Biosynthesis and secretion of human interleukin-2 glycoprotein variants from baculovirus-infected Sf-21 cells. Eur. J. Biochem., 215, 189-197.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 189-197
    • Grabenhorst, E.1    Hofler, B.2    Nimtz, M.3    Jager, V.4    Conrad, H.S.5
  • 20
    • 0028097855 scopus 로고
    • The core-specific Iysosomal α(1-6)-mannosidase activity depends on aspartamidohydrolase activity
    • Haeuw, J.F., Grard, T., Alonso, C., Strecker, G. and Michalski, J.C. (1994) The core-specific Iysosomal α(1-6)-mannosidase activity depends on aspartamidohydrolase activity. Biochem. J., 294, 463-466.
    • (1994) Biochem. J. , vol.294 , pp. 463-466
    • Haeuw, J.F.1    Grard, T.2    Alonso, C.3    Strecker, G.4    Michalski, J.C.5
  • 21
    • 0027405920 scopus 로고
    • Structure of the Asn-linked oligosaccharides of apolipoprotein III from the insect Locusta migraforia. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein
    • Hard, K., Van Doorn, J.M., Thomas-Oates, J.E., Kamerling, J.P. and Van Der Horst, D.J. (1993) Structure of the Asn-linked oligosaccharides of apolipoprotein III from the insect Locusta migraforia. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein. Biochemistry, 32, 766-775.
    • (1993) Biochemistry , vol.32 , pp. 766-775
    • Hard, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van Der Horst, D.J.5
  • 22
    • 0028167059 scopus 로고
    • Mass spectrometric studies on the N-linked oligosaccharides of baculovirus expressed mouse interleukine-3
    • Hogeland, K.E., Jr, and Deinzer, M.L. (1994) Mass spectrometric studies on the N-linked oligosaccharides of baculovirus expressed mouse interleukine-3. Biol. Mass Spectrometry, 23, 218-224.
    • (1994) Biol. Mass Spectrometry , vol.23 , pp. 218-224
    • Hogeland Jr., K.E.1    Deinzer, M.L.2
  • 23
    • 0015452895 scopus 로고
    • Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds
    • Houmard, J. and Drapeau, G.R. (1972) Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc. Natl. Acad. Sci. USA, 69, 3506-3509.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3506-3509
    • Houmard, J.1    Drapeau, G.R.2
  • 24
    • 0021770329 scopus 로고
    • Regulation of asparagine-linked oligosaccharide processing: Oligosaccharide processing in Aedes albopictus mosquito cells
    • Hsieh, P. and Robbins, P.W. (1984) Regulation of asparagine-linked oligosaccharide processing: oligosaccharide processing in Aedes albopictus mosquito cells. J. Biol. Chem., 259, 2375-2382.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2375-2382
    • Hsieh, P.1    Robbins, P.W.2
  • 25
    • 0024574726 scopus 로고
    • Glycosylation and secretion of human tissue plasminogen activator in recombinant baculovirus-infected insect cells
    • Jarvis, D.L. and Summers, M.D. (1989) Glycosylation and secretion of human tissue plasminogen activator in recombinant baculovirus-infected insect cells. Mol. Cell. Biol., 9, 214-223.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 214-223
    • Jarvis, D.L.1    Summers, M.D.2
  • 26
    • 0025305021 scopus 로고
    • Role of glycosylation in the transport of recombinant glycoproteins through the secretory pathway of lepidopteran insect cells
    • Jarvis, D.L., Oker-Blom, C. and Summers, M.D. (1990) Role of glycosylation in the transport of recombinant glycoproteins through the secretory pathway of lepidopteran insect cells. J. Cell Biochem., 42, 181-191.
    • (1990) J. Cell Biochem. , vol.42 , pp. 181-191
    • Jarvis, D.L.1    Oker-Blom, C.2    Summers, M.D.3
  • 27
    • 0028910204 scopus 로고
    • Glycosylation of proteins. Monitoring and control of recombinant glycoprotein heterogeneity in animal cell cultures
    • Jenkins, N. (1995) Glycosylation of proteins. Monitoring and control of recombinant glycoprotein heterogeneity in animal cell cultures. Biochem. Soc. Trans., 23, 171-175.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 171-175
    • Jenkins, N.1
  • 28
    • 0016758296 scopus 로고
    • Characterization by gas-liquid chromatography-mass spectrometry and proton-magnetic-resonance spectroscopy of permethysilyl methyl glycosides obtained in methanolysis of glycoproteins and glycopeptides
    • Kamerling, J.P., Gerwig, G.J., Vliegenthart, J.F.G. and Clamp, J.R. (1975) Characterization by gas-liquid chromatography-mass spectrometry and proton-magnetic-resonance spectroscopy of permethysilyl methyl glycosides obtained in methanolysis of glycoproteins and glycopeptides. Biochem. J., 151, 491-495.
    • (1975) Biochem. J. , vol.151 , pp. 491-495
    • Kamerling, J.P.1    Gerwig, G.J.2    Vliegenthart, J.F.G.3    Clamp, J.R.4
  • 29
    • 0024223084 scopus 로고
    • Baculovirus vectors for expression of foreign genes
    • Kang, C.Y. (1988) Baculovirus vectors for expression of foreign genes. Adv. Virus Res., 35, 177-192.
    • (1988) Adv. Virus Res. , vol.35 , pp. 177-192
    • Kang, C.Y.1
  • 30
    • 9244228605 scopus 로고
    • Influence of glycosylation on antigenicity of viral proteins
    • van Regenmortel, M.H.V. and Neurath, A.R. (eds.), Elsevier Science Publishers, Amsterdam
    • Klenk, H.-D. (1990) Influence of glycosylation on antigenicity of viral proteins, In van Regenmortel, M.H.V. and Neurath, A.R. (eds.), Immunochemistry of Viruses. II. The Basis of Serodiagnosis and Vaccines. Elsevier Science Publishers, Amsterdam, pp. 25-37.
    • (1990) Immunochemistry of Viruses. II. The Basis of Serodiagnosis and Vaccines , pp. 25-37
    • Klenk, H.-D.1
  • 31
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata, A. (1992) Structures and functions of the sugar chains of glycoproteins. Eur. J. Biochem., 209, 483-501
    • (1992) Eur. J. Biochem. , vol.209 , pp. 483-501
    • Kobata, A.1
  • 32
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 34
    • 0028236119 scopus 로고
    • Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N)
    • Kubelka, V., Altmann, F., Kornfeld, G. and März, L. (1994) Structures of the N-linked oligosaccharides of the membrane glycoproteins from three lepidopteran cell lines (Sf-21, IZD-Mb-0503, Bm-N). Arch. Biochem. Biophys., 308, 148-157.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 148-157
    • Kubelka, V.1    Altmann, F.2    Kornfeld, G.3    März, L.4
  • 35
    • 0022729887 scopus 로고
    • Expression of the influenza virus hemagglutinin in insect cells by a baculovirus vector
    • Kuroda, K., Hauser, C., Rott, R., Klenk, H.-D. and Doerfler, W. (1986) Expression of the influenza virus hemagglutinin in insect cells by a baculovirus vector. EMBO J., 5, 1359-1365.
    • (1986) EMBO J. , vol.5 , pp. 1359-1365
    • Kuroda, K.1    Hauser, C.2    Rott, R.3    Klenk, H.-D.4    Doerfler, W.5
  • 37
    • 0025193736 scopus 로고
    • The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector
    • Kuroda, K., Geyer, H., Geyer, R., Doerfler, W. and Klenk, H.-D. (1990) The oligosaccharides of influenza virus hemagglutinin expressed in insect cells by a baculovirus vector. Virology, 174, 418-429.
    • (1990) Virology , vol.174 , pp. 418-429
    • Kuroda, K.1    Geyer, H.2    Geyer, R.3    Doerfler, W.4    Klenk, H.-D.5
  • 38
    • 0025956827 scopus 로고
    • Retarded processing of influenza virus hemagglutinin in insect cells
    • Kuroda, K., Veit, M. and Klenk, H.-D. (1991) Retarded processing of influenza virus hemagglutinin in insect cells. Virology, 180, 159-165.
    • (1991) Virology , vol.180 , pp. 159-165
    • Kuroda, K.1    Veit, M.2    Klenk, H.-D.3
  • 39
    • 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
  • 40
    • 0027561440 scopus 로고
    • Insect cell hosts for baculovirus expression vectors contain endogenous exoglycosidase activity
    • Licari, P.J., Jarvis, D.L. and Bailey, J.E. (1993) Insect cell hosts for baculovirus expression vectors contain endogenous exoglycosidase activity. Biotechnol. Prog., 9, 146-152.
    • (1993) Biotechnol. Prog. , vol.9 , pp. 146-152
    • Licari, P.J.1    Jarvis, D.L.2    Bailey, J.E.3
  • 41
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis, H. and Sharon, N. (1993) Protein glycosylation. Structural and functional aspects. Eur. J. Biochem., 218, 1-27.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 42
    • 0023881356 scopus 로고
    • Trends in the development of baculovirus expression vectors
    • Luckow, V.A and Summers, M.D. (1988) Trends in the development of baculovirus expression vectors. Bio/Technology, 6, 47-55.
    • (1988) Bio/Technology , vol.6 , pp. 47-55
    • Luckow, V.A.1    Summers, M.D.2
  • 43
    • 0028117390 scopus 로고
    • Structural analysis and localization of the carbohydrate moieties of the soluble human interferon receptor produced in baculovirus-infected insect cells
    • Manneberg, M., Friedlein, A., Kurth, H., Lahm, H.-W. and Fountoulakis, M. (1994) Structural analysis and localization of the carbohydrate moieties of the soluble human interferon receptor produced in baculovirus-infected insect cells. Protein Sci., 3, 30-38.
    • (1994) Protein Sci. , vol.3 , pp. 30-38
    • Manneberg, M.1    Friedlein, A.2    Kurth, H.3    Lahm, H.-W.4    Fountoulakis, M.5
  • 44
    • 77956668614 scopus 로고    scopus 로고
    • Chapter 1b: Normal and pathological catabolism of glycoproteins
    • Montreuil, J., Vliegenthart, J.F.G. and Schachter, H. (eds.), Elsevier Science, Amsterdam
    • Michalski, J.C. (1996) Chapter 1b: normal and pathological catabolism of glycoproteins, In: Montreuil, J., Vliegenthart, J.F.G. and Schachter, H. (eds.), Glycoproteins and Disease. Elsevier Science, Amsterdam, pp. 55-97
    • (1996) Glycoproteins and Disease , pp. 55-97
    • Michalski, J.C.1
  • 45
    • 0024152865 scopus 로고
    • Baculoviruses as gene expression vectors
    • Miller, L.K. (1988) Baculoviruses as gene expression vectors. Annu. Rev. Microbiol., 42, 177-199.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 177-199
    • Miller, L.K.1
  • 46
    • 0026642422 scopus 로고
    • Carbohydrate masking of an antigenic epitope of influenza virus hemagglutinin independent of oligosaccharide size
    • Munk, K., Pritzer, E., Kretzschmar, E., Gutte, B., Garten, W. and Klenk, H.-D. (1992) Carbohydrate masking of an antigenic epitope of influenza virus hemagglutinin independent of oligosaccharide size. Glycobiology, 2, 233-240.
    • (1992) Glycobiology , vol.2 , pp. 233-240
    • Munk, K.1    Pritzer, E.2    Kretzschmar, E.3    Gutte, B.4    Garten, W.5    Klenk, H.-D.6
  • 47
    • 0345036792 scopus 로고
    • Immunogenic properties of avian leukosis virus env-proteins synthesized with a baculovirus expression vector
    • Vlak, J.M., Schlaeger, E.-J. and Bernard, A.R. (eds.), Editiones Roche, Basel
    • Noteborn, M.H.M., Kant, A., Eijdems, E.W.H.M., De Boer, G.F., Van Der Eb, A.J. and Koch, G. (1992) Immunogenic properties of avian leukosis virus env-proteins synthesized with a baculovirus expression vector. In Vlak, J.M., Schlaeger, E.-J. and Bernard, A.R. (eds.), Workshop on Baculovirus and Recombinant Protein Production Processes. Editiones Roche, Basel, pp. 92-97.
    • (1992) Workshop on Baculovirus and Recombinant Protein Production Processes , pp. 92-97
    • Noteborn, M.H.M.1    Kant, A.2    Eijdems, E.W.H.M.3    De Boer, G.F.4    Van Der Eb, A.J.5    Koch, G.6
  • 48
    • 0030070842 scopus 로고    scopus 로고
    • Isolation and characterization of an insect cell line able to perform complex N-linked glycosylation on recombinant proteins
    • Ogonah, W.O., Freedman, R.B., Jenkins, N., Patel, K. and Rooney, B.C. (1996) Isolation and characterization of an insect cell line able to perform complex N-linked glycosylation on recombinant proteins. Bio/Technology, 14, 197-202.
    • (1996) Bio/Technology , vol.14 , pp. 197-202
    • Ogonah, W.O.1    Freedman, R.B.2    Jenkins, N.3    Patel, K.4    Rooney, B.C.5
  • 49
    • 0020323208 scopus 로고
    • Carbohydrate moieties of glycoproteins. A reevaluation of their function
    • Olden, K., Parent, J.B. and White, S.L. (1982) Carbohydrate moieties of glycoproteins. A reevaluation of their function. Biochim. Biophys. Acta, 650, 209-232.
    • (1982) Biochim. Biophys. Acta , vol.650 , pp. 209-232
    • Olden, K.1    Parent, J.B.2    White, S.L.3
  • 51
    • 0041660995 scopus 로고
    • Refined chemical techniques for the quantitative recovery of intact N- and O-linked oligosaccharides from glycoproteins
    • Parekh, R.B., Warren, C.E., Merry, A. and Bruce, J. (1990) Refined chemical techniques for the quantitative recovery of intact N- and O-linked oligosaccharides from glycoproteins. Glycoconjugate J., 7, 382-383.
    • (1990) Glycoconjugate J. , vol.7 , pp. 382-383
    • Parekh, R.B.1    Warren, C.E.2    Merry, A.3    Bruce, J.4
  • 52
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins
    • Patel, T., Bruce, J., Merry, A., Bigge, C., Wormald, M., Jacques, A. and Parekh, R.B. (1993) Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry, 32, 679-693.
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jacques, A.6    Parekh, R.B.7
  • 54
    • 0028293504 scopus 로고
    • Expression of the Sendai virus fusion protein in insect cells and characterization of its posttranslational modifications
    • Ponimaskin, E., Veit, M. and Schmidt, M.F.G. (1994) Expression of the Sendai virus fusion protein in insect cells and characterization of its posttranslational modifications. J. Gen. Virol., 75, 1163-1167.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1163-1167
    • Ponimaskin, E.1    Veit, M.2    Schmidt, M.F.G.3
  • 56
    • 0026049185 scopus 로고
    • The "yellow brick road" to branched complex N-glycans
    • Schachter, H. (1991) The "yellow brick road" to branched complex N-glycans. Glycobiology, 1, 453-461.
    • (1991) Glycobiology , vol.1 , pp. 453-461
    • Schachter, H.1
  • 58
    • 0026426731 scopus 로고
    • Sticky sugars for selectins
    • Springer, T.A. and Lasley, L.A. (1991) Sticky sugars for selectins. Nature, 349, 196-197.
    • (1991) Nature , vol.349 , pp. 196-197
    • Springer, T.A.1    Lasley, L.A.2
  • 60
    • 0026734854 scopus 로고
    • Distinct N-glycan fucosylation potentials of three lepidopteran cell lines
    • Staudacher, E., Kubelka, V. and März, L. (1992b) Distinct N-glycan fucosylation potentials of three lepidopteran cell lines. Eur. J. Biochem., 207, 987-993.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 987-993
    • Staudacher, E.1    Kubelka, V.2    März, L.3
  • 61
    • 0001962451 scopus 로고
    • A manual methods for baculovirus vectors and insect cell culture procedures
    • Summers, M.D. and Smith, G.E. (1987) a manual methods for baculovirus vectors and insect cell culture procedures. Tex. Agric. Exp. Stn. Bull., 1555.
    • (1987) Tex. Agric. Exp. Stn. Bull. , vol.1555
    • Summers, M.D.1    Smith, G.E.2
  • 62
    • 20644439227 scopus 로고
    • Structures and fonction roles of the sugar chains of human erytropoietins
    • Takeuchi, M. and Kobata, A. (1991) Structures and fonction roles of the sugar chains of human erytropoietins. Glycobiology, 349, 196-197.
    • (1991) Glycobiology , vol.349 , pp. 196-197
    • Takeuchi, M.1    Kobata, A.2
  • 63
    • 0029877528 scopus 로고    scopus 로고
    • Glycosylation in lepidopteran insect cells: Identification of a β1 4-N-acetylgalactosyl-transferase involved in the synthesis of complex-type oligosaccharide chains
    • Van Die, I., Van Tetering, A., Bakker, H., Van den Eijnden, D.H. and Joziasse, D.H (1996) Glycosylation in lepidopteran insect cells: identification of a β1 4-N-acetylgalactosyl-transferase involved in the synthesis of complex-type oligosaccharide chains. Glycobiology, 6, 157-164.
    • (1996) Glycobiology , vol.6 , pp. 157-164
    • Van Die, I.1    Van Tetering, A.2    Bakker, H.3    Van Den Eijnden, D.H.4    Joziasse, D.H.5
  • 64
    • 0343255342 scopus 로고
    • Jones, C., Mulloy, B. and Thomas, A.H. (eds.), Humana Press, Totowa
    • Van Halbeek, H. (1993) In Jones, C., Mulloy, B. and Thomas, A.H. (eds.), Methods in Molecular Biology, Vol. 17. Humana Press, Totowa, pp. 115-148.
    • (1993) Methods in Molecular Biology , vol.17 , pp. 115-148
    • Van Halbeek, H.1
  • 65
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 66
    • 0027145389 scopus 로고
    • Structure, function, and intracellular localization of glycoprotein B of herpes virus simian agent 8 expressed in insect and mammalian cells
    • Veit, M., Scott, C., Borchers, K., Ludwig, H. and Schmidt, M.F.G. (1993) Structure, function, and intracellular localization of glycoprotein B of herpes virus simian agent 8 expressed in insect and mammalian cells. Arch Virol., 133, 335-347.
    • (1993) Arch Virol. , vol.133 , pp. 335-347
    • Veit, M.1    Scott, C.2    Borchers, K.3    Ludwig, H.4    Schmidt, M.F.G.5
  • 67
    • 0027282196 scopus 로고
    • The presence of UDP-N-acetylglucosamine:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I activity in Spodoptera frugiperda cells (IPLB-Sf-21AE) and its enhancement as a result of baculovirus infection
    • Velardo, M.A., Bretthauer, R.K., Boutaud, A., Reinhold, B., Reinhold, V.N. and Castellino, F.J. (1993) The presence of UDP-N-acetylglucosamine:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I activity in Spodoptera frugiperda cells (IPLB-Sf-21AE) and its enhancement as a result of baculovirus infection. J. Biol. Chem., 268, 17902-17907.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17902-17907
    • Velardo, M.A.1    Bretthauer, R.K.2    Boutaud, A.3    Reinhold, B.4    Reinhold, V.N.5    Castellino, F.J.6
  • 68
    • 0343373375 scopus 로고
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins. Adv. Carbohydr. Chem. Biochem., 41, 209-374.
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 209-374
    • Vliegenthart, J.F.G.1    Dorland, L.2    Van Halbeek, H.3
  • 69
    • 0027381117 scopus 로고
    • Expression of human interferon ω1 in Sf-9 cells. No evidence for complex-type N-linked glycosylation or sialylation
    • Voss, T., Ergülen, E., Ahorn, H., Kubelka, V., Sugiyama, K., Maurer-Fogy, I. and Glössl, J. (1993) Expression of human interferon ω1 in Sf-9 cells. No evidence for complex-type N-linked glycosylation or sialylation. Eur. J. Biochem., 217, 913-919.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 913-919
    • Voss, T.1    Ergülen, E.2    Ahorn, H.3    Kubelka, V.4    Sugiyama, K.5    Maurer-Fogy, I.6    Glössl, J.7
  • 70
    • 0025726262 scopus 로고
    • Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in insect cell line Sf-9
    • Wathen, M.W., Aeed, P.A. and Elhammer, A.P. (1991) Characterization of oligosaccharide structures on a chimeric respiratory syncytial virus protein expressed in insect cell line Sf-9. Biochemistry, 30, 2863-2868.
    • (1991) Biochemistry , vol.30 , pp. 2863-2868
    • Wathen, M.W.1    Aeed, P.A.2    Elhammer, A.P.3
  • 72
    • 0028931761 scopus 로고
    • Stable secretion of a soluble oligomeric form of rabies virus glycoprotein: Influence of N-glycan. Processing on secretion
    • Wojczyk, B., Shakin-Eshleman, S.H., Doms, R.W., Xiang, Z.Q., Ertl, H.C.J., Wunner, W.H. and Spitalnik, S.L. (1995) Stable secretion of a soluble oligomeric form of rabies virus glycoprotein: influence of N-glycan. Processing on secretion. Biochemistry, 34, 2599-2609.
    • (1995) Biochemistry , vol.34 , pp. 2599-2609
    • Wojczyk, B.1    Shakin-Eshleman, S.H.2    Doms, R.W.3    Xiang, Z.Q.4    Ertl, H.C.J.5    Wunner, W.H.6    Spitalnik, S.L.7
  • 73
    • 0027508349 scopus 로고
    • Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system
    • Yeh, J., Seals, J.R., Murphy, C.I., van Halbeek, H. and Cummings, R.D. (1993) Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry, 32, 11087-11099.
    • (1993) Biochemistry , vol.32 , pp. 11087-11099
    • Yeh, J.1    Seals, J.R.2    Murphy, C.I.3    Van Halbeek, H.4    Cummings, R.D.5
  • 74
    • 0015494930 scopus 로고
    • Analysis of monosaccharides by gas-liquid chromatography of the O-methyl glycosides as trifluoroacetate derivatives. Application to glycoproteins and glycolipids
    • Zanetta, J.P., Breckenridge, S.C. and Vincendon, G. (1972) Analysis of monosaccharides by gas-liquid chromatography of the O-methyl glycosides as trifluoroacetate derivatives. Application to glycoproteins and glycolipids. J. Chromatogr., 69, 291-304.
    • (1972) J. Chromatogr. , vol.69 , pp. 291-304
    • Zanetta, J.P.1    Breckenridge, S.C.2    Vincendon, G.3


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