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Volumn 6, Issue 7, 2008, Pages 733-748

Considerations for extraction of monoclonal antibodies targeted to different subcellular compartments in transgenic tobacco plants

Author keywords

Extraction; Leaves; Monoclonal antibody; Tobacco; Transgenic

Indexed keywords

HYBRID PROTEIN; MONOCLONAL ANTIBODY; VEGETABLE PROTEIN;

EID: 49349095531     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/j.1467-7652.2008.00354.x     Document Type: Article
Times cited : (65)

References (69)
  • 2
    • 0028308081 scopus 로고
    • Separation and purification of recombinant proteins from Escherichia coli with aqueous two-phase systems
    • Asenjo, J.A., Turner, R.E., Mistry, S.L. Kaul, A. (1994) Separation and purification of recombinant proteins from Escherichia coli with aqueous two-phase systems. J. Chromatogr. A, 668, 129 137.
    • (1994) J. Chromatogr. a , vol.668 , pp. 129-137
    • Asenjo, J.A.1    Turner, R.E.2    Mistry, S.L.3    Kaul, A.4
  • 3
    • 0037027397 scopus 로고    scopus 로고
    • Recombinant aprotinin produced in transgenic corn seed: Extraction and purification studies
    • Azzoni, A.R., Kusnadi, A.R., Miranda, E.A. Nikolov, Z.L. (2002) Recombinant aprotinin produced in transgenic corn seed: extraction and purification studies. Biotechnol. Bioeng. 80, 268 276.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 268-276
    • Azzoni, A.R.1    Kusnadi, A.R.2    Miranda, E.A.3    Nikolov, Z.L.4
  • 4
    • 14144253431 scopus 로고    scopus 로고
    • Transgenic corn seed for recombinant protein production: Relevant aspects on the aqueous extraction of native components
    • Azzoni, A.R., Farinas, C.S. Miranda, E.A. (2005) Transgenic corn seed for recombinant protein production: relevant aspects on the aqueous extraction of native components. J. Sci. Food Agric. 85, 609 614.
    • (2005) J. Sci. Food Agric. , vol.85 , pp. 609-614
    • Azzoni, A.R.1    Farinas, C.S.2    Miranda, E.A.3
  • 5
    • 0018786476 scopus 로고
    • Structural determinants of Concanavalin a specificity for oligosaccharides
    • Baenziger, J.U. Fiete, D. (1979) Structural determinants of Concanavalin A specificity for oligosaccharides. J. Biol. Chem. 254, 2400 2407.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2400-2407
    • Baenziger, J.U.1    Fiete, D.2
  • 6
    • 0035128474 scopus 로고    scopus 로고
    • Effect of processing on the recovery of recombinant β-glucuronidase (rGUS) from transgenic canola
    • Bai, Y. Nikolov, Z.L. (2001) Effect of processing on the recovery of recombinant β-glucuronidase (rGUS) from transgenic canola. Biotechnol. Prog. 17, 168 174.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 168-174
    • Bai, Y.1    Nikolov, Z.L.2
  • 8
    • 0036115870 scopus 로고    scopus 로고
    • Biochemical analysis of transgenic tobacco lines producing bacterial serine acetyltransferase
    • Blaszczyk, A., Sirko, L., Hawkesford, M.J. Sirko, A. (2002) Biochemical analysis of transgenic tobacco lines producing bacterial serine acetyltransferase. Plant Sci. 162, 589 597.
    • (2002) Plant Sci. , vol.162 , pp. 589-597
    • Blaszczyk, A.1    Sirko, L.2    Hawkesford, M.J.3    Sirko, A.4
  • 9
    • 0037143782 scopus 로고    scopus 로고
    • Ultra scale-down to predict filtering centrifugation of secreted antibody fragments from fungal broth
    • Boulding, N., Yim, S.S.S., Keshavarz-Moore, E., Ayazi Shamlou, P. Berry, M. (2002) Ultra scale-down to predict filtering centrifugation of secreted antibody fragments from fungal broth. Biotechnol. Bioeng. 79, 381 388.
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 381-388
    • Boulding, N.1    Yim, S.S.S.2    Keshavarz-Moore, E.3    Ayazi Shamlou, P.4    Berry, M.5
  • 10
    • 0030963217 scopus 로고    scopus 로고
    • Clearance ratios of amylase isoenzymes and IgG subclasses: Do they reflect glomerular charge selectivity?
    • Buis, B., Wever, P.C., Koomen, G.C., van Acker, B.A., Groothoff, J.W., Krediet, R.T. Arisz, L. (1997) Clearance ratios of amylase isoenzymes and IgG subclasses: do they reflect glomerular charge selectivity? Nephron, 75, 444 450.
    • (1997) Nephron , vol.75 , pp. 444-450
    • Buis, B.1    Wever, P.C.2    Koomen, G.C.3    Van Acker, B.A.4    Groothoff, J.W.5    Krediet, R.T.6    Arisz, L.7
  • 12
    • 0033805614 scopus 로고    scopus 로고
    • A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice
    • Chargelegue, D., Vine, N.D., van Dolleweerd, C.J., Drake, P.M.W. Ma, J.K.-C. (2000) A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice. Transgenic Res. 9, 187 194.
    • (2000) Transgenic Res. , vol.9 , pp. 187-194
    • Chargelegue, D.1    Vine, N.D.2    Van Dolleweerd, C.J.3    Drake, P.M.W.4    Ma, J.K.-C.5
  • 13
    • 0019299557 scopus 로고
    • Phytic acid interactions in food systems
    • Cheryan, M. (1980) Phytic acid interactions in food systems. Crit. Rev. Food Sci. Nutr. 13, 297 335.
    • (1980) Crit. Rev. Food Sci. Nutr. , vol.13 , pp. 297-335
    • Cheryan, M.1
  • 14
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity
    • Conrad, U. Fiedler, U. (1998) Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity. Plant Mol. Biol. 38, 101 109.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 15
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • Denecke, J., De Rycke, R. Botterman, J. (1992) Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 11, 2345 2355.
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    De Rycke, R.2    Botterman, J.3
  • 16
    • 0036929331 scopus 로고    scopus 로고
    • Expression and affinity purification of recombinant proteins from plants
    • Desai, U., Sur, G., Daunert, S., Babbit, T.R. Li, Q. (2002) Expression and affinity purification of recombinant proteins from plants. Prot. Expression Purif. 25, 195 202.
    • (2002) Prot. Expression Purif. , vol.25 , pp. 195-202
    • Desai, U.1    Sur, G.2    Daunert, S.3    Babbit, T.R.4    Li, Q.5
  • 17
    • 0037307435 scopus 로고    scopus 로고
    • Characterization of the conformational epitope of Guy's 13, a monoclonal antibody that prevents Streptococcus mutans colonization in humans
    • van Dolleweerd, C.J., Chargelegue, D. Ma, J.K.-C. (2003) Characterization of the conformational epitope of Guy's 13, a monoclonal antibody that prevents Streptococcus mutans colonization in humans. Infect. Immun. 71, 754 765.
    • (2003) Infect. Immun. , vol.71 , pp. 754-765
    • Van Dolleweerd, C.J.1    Chargelegue, D.2    Ma, J.K.-C.3
  • 19
    • 0032127253 scopus 로고    scopus 로고
    • Process and economic evaluation of the extraction and purification of recombinant β-glucuronidase from transgenic corn
    • Evangelista, R.L., Kusnadi, A.R., Howard, J.A. Nikolov, Z.L. (1998) Process and economic evaluation of the extraction and purification of recombinant β-glucuronidase from transgenic corn. Biotechnol. Prog. 14, 607 614.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 607-614
    • Evangelista, R.L.1    Kusnadi, A.R.2    Howard, J.A.3    Nikolov, Z.L.4
  • 22
    • 34147095513 scopus 로고    scopus 로고
    • Viral vectors for the expression of proteins in plants
    • Gleba, Y., Klimyuk, V. Marillonnet, S. (2007) Viral vectors for the expression of proteins in plants. Curr. Opin. Biotechnol. 18, 134 141.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 134-141
    • Gleba, Y.1    Klimyuk, V.2    Marillonnet, S.3
  • 24
    • 0026761132 scopus 로고
    • PH-sensitive interactions between IgG and a mutated IgG-binding protein based upon two B domains of Protein a from Staphylococcus aureus
    • Gore, M.G., Ferris, W.F., Popplewell, A.G., Scawen, M. Atkinson, T. (1992) pH-sensitive interactions between IgG and a mutated IgG-binding protein based upon two B domains of Protein A from Staphylococcus aureus. Protein Eng. 5, 577 582.
    • (1992) Protein Eng. , vol.5 , pp. 577-582
    • Gore, M.G.1    Ferris, W.F.2    Popplewell, A.G.3    Scawen, M.4    Atkinson, T.5
  • 25
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A. Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019 1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 26
    • 0020574525 scopus 로고
    • A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid
    • 180.
    • Hoekema, A., Hirsch, P.R., Hooykaas, P.J.J. Schilperoort, R.A. (1983) A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid. Nature, 303, 179 180.
    • (1983) Nature , vol.303 , pp. 179
    • Hoekema, A.1    Hirsch, P.R.2    Hooykaas, P.J.J.3    Schilperoort, R.A.4
  • 27
    • 39549092440 scopus 로고    scopus 로고
    • Purification of an acidic recombinant protein from transgenic tobacco
    • Holler, C. Zhang, C. (2008) Purification of an acidic recombinant protein from transgenic tobacco. Biotechnol. Bioeng. 99, 902 909.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 902-909
    • Holler, C.1    Zhang, C.2
  • 28
    • 33846575577 scopus 로고    scopus 로고
    • Polyethyleneimine precipitation versus anion exchange chromatography in fractionating recombinant beta-glucuronidase from transgenic tobacco extract
    • Holler, C., Vaughan, D. Zhang, C. (2007) Polyethyleneimine precipitation versus anion exchange chromatography in fractionating recombinant beta-glucuronidase from transgenic tobacco extract. J. Chromatogr. A, 1142, 98 105.
    • (2007) J. Chromatogr. a , vol.1142 , pp. 98-105
    • Holler, C.1    Vaughan, D.2    Zhang, C.3
  • 29
    • 0022382844 scopus 로고
    • Inactivation of viruses in labile blood derivatives
    • Horowitz, B., Wiebe, M.E., Lippin, A. Stryker, M.H. (1985) Inactivation of viruses in labile blood derivatives. Transfusion, 25, 516 522.
    • (1985) Transfusion , vol.25 , pp. 516-522
    • Horowitz, B.1    Wiebe, M.E.2    Lippin, A.3    Stryker, M.H.4
  • 31
    • 23844547597 scopus 로고    scopus 로고
    • Engineering mammalian cell factories for improved recombinant monoclonal antibody production: Lessons from nature?
    • James, D.C. Dinnis, D.M. (2005) Engineering mammalian cell factories for improved recombinant monoclonal antibody production: lessons from nature? Biotechnol. Bioeng. 91, 180 189.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 180-189
    • James, D.C.1    Dinnis, D.M.2
  • 32
    • 0024716141 scopus 로고
    • Purification technologies for plant-proteins
    • Jervis, L. Pierpoint, W.S. (1989) Purification technologies for plant-proteins. J. Biotechnol. 11, 161 198.
    • (1989) J. Biotechnol. , vol.11 , pp. 161-198
    • Jervis, L.1    Pierpoint, W.S.2
  • 33
    • 0023236892 scopus 로고
    • Duplication of CaMV-35S promoter sequences creates a strong enhancer for plant genes
    • Kay, R., Chan, A., Daly, M. McPherson, J. (1987) Duplication of CaMV-35S promoter sequences creates a strong enhancer for plant genes. Science, 236, 1299 1302.
    • (1987) Science , vol.236 , pp. 1299-1302
    • Kay, R.1    Chan, A.2    Daly, M.3    McPherson, J.4
  • 35
    • 0032487368 scopus 로고    scopus 로고
    • Processing of transgenic corn seed and its effect on the recovery of recombinant beta-glucuronidase
    • Kusnadi, A.R., Evangelista, R.L., Hood, E.E., Howard, J.A. Nikolov, Z.L. (1998a) Processing of transgenic corn seed and its effect on the recovery of recombinant beta-glucuronidase. Biotechnol. Bioeng. 60, 44 52.
    • (1998) Biotechnol. Bioeng. , vol.60 , pp. 44-52
    • Kusnadi, A.R.1    Evangelista, R.L.2    Hood, E.E.3    Howard, J.A.4    Nikolov, Z.L.5
  • 37
    • 0036007990 scopus 로고    scopus 로고
    • Mechanical stability of immobilized biocatalysts (CLECs) in dilute agitated suspensions
    • Lee, T.S., Turner, M.K. Lye, G.J. (2002) Mechanical stability of immobilized biocatalysts (CLECs) in dilute agitated suspensions. Biotechnol. Prog. 18, 43 50.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 43-50
    • Lee, T.S.1    Turner, M.K.2    Lye, G.J.3
  • 38
    • 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. 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
  • 40
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma, J.K.-C., Hikmat, B.Y., Wycoff, K., Vine, N.D., Chargelegue, D., Yu, L., Hein, M.B. Lehner, T. (1998) Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nature Med. 4, 601 606.
    • (1998) Nature Med. , vol.4 , pp. 601-606
    • Ma, J.K.-C.1    Hikmat, B.Y.2    Wycoff, K.3    Vine, N.D.4    Chargelegue, D.5    Yu, L.6    Hein, M.B.7    Lehner, T.8
  • 41
    • 0141706699 scopus 로고    scopus 로고
    • The production of pharmaceutical proteins in plants
    • Ma, J.K.-C., Drake, P.M.W. Christou, P. (2003) The production of pharmaceutical proteins in plants. Nat. Rev. Genet. 4, 794 805.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 794-805
    • Ma, J.K.-C.1    Drake, P.M.W.2    Christou, P.3
  • 42
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Maire, M.L., Champeil, P. Møller, J.V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta. 1508, 86 111.
    • (2000) Biochim. Biophys. Acta. , vol.1508 , pp. 86-111
    • Maire, M.L.1    Champeil, P.2    Møller, J.V.3
  • 43
    • 0027048769 scopus 로고
    • Expression of hepatitis B surface antigen in transgenic plants
    • Mason, H.S., Lam, D.M.K. Arntzen, C.J. (1992) Expression of hepatitis B surface antigen in transgenic plants. Proc. Natl. Acad. Sci. USA, 89, 11 745 11 749.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11745-11749
    • Mason, H.S.1    Lam, D.M.K.2    Arntzen, C.J.3
  • 44
    • 49349093724 scopus 로고    scopus 로고
    • Compatibility of column inlet and adsorbent designs for processing of corn endosperm extracts by packed bed and expanded bed adsorption
    • Menkhaus, T.J. Glatz, C.E. (2004a) Compatibility of column inlet and adsorbent designs for processing of corn endosperm extracts by packed bed and expanded bed adsorption. Biotechnol. Bioeng. 20, 1001 1014.
    • (2004) Biotechnol. Bioeng. , vol.20 , pp. 1001-1014
    • Menkhaus, T.J.1    Glatz, C.E.2
  • 45
    • 0034115723 scopus 로고    scopus 로고
    • The industrial production cost of recombinant therapeutic proteins expressed in transgenic corn.
    • Mison, D. Curling, J. (2000) The industrial production cost of recombinant therapeutic proteins expressed in transgenic corn. Biopharm. 13, 48 54.
    • (2000) Biopharm. , vol.13 , pp. 48-54
    • Mison, D.1    Curling, J.2
  • 46
    • 0008203189 scopus 로고
    • The effect of shear on globular proteins during ultrafiltration; Studies of alcohol dehydrogenase
    • Narendranathan, T.J. Dunnill, P. (1982) The effect of shear on globular proteins during ultrafiltration; studies of alcohol dehydrogenase. Biotechnol. Bioeng, 24, 2103 2107.
    • (1982) Biotechnol. Bioeng , vol.24 , pp. 2103-2107
    • Narendranathan, T.J.1    Dunnill, P.2
  • 47
    • 0037454676 scopus 로고    scopus 로고
    • Ultra scale-down approach for the prediction of full-scale recovery of ovine polyclonal immunoglobulins used in the manufacture of snake venom-specific Fab fragment
    • Neal, G., Christie, J., Keshavarz-Moore, E. Shamlou, P.A. (2003) Ultra scale-down approach for the prediction of full-scale recovery of ovine polyclonal immunoglobulins used in the manufacture of snake venom-specific Fab fragment. Biotechnol. Bioeng. 81, 149 157.
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 149-157
    • Neal, G.1    Christie, J.2    Keshavarz-Moore, E.3    Shamlou, P.A.4
  • 48
    • 0037394628 scopus 로고    scopus 로고
    • Chemically regulated gene expression in plants
    • Padidam, M. (2003) Chemically regulated gene expression in plants. Curr. Opin. Plant Biol. 6, 169 177.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 169-177
    • Padidam, M.1
  • 52
    • 77957060270 scopus 로고
    • Improved vectors for plant transformation: Expression cassette vectors and new selectable markers
    • Rogers, S.G., Klee, H.J., Horsch, R.B. Fraley, R.T. (1987) Improved vectors for plant transformation: expression cassette vectors and new selectable markers. Methods Enzymol. 153, 253 277.
    • (1987) Methods Enzymol. , vol.153 , pp. 253-277
    • Rogers, S.G.1    Klee, H.J.2    Horsch, R.B.3    Fraley, R.T.4
  • 53
    • 1642634947 scopus 로고    scopus 로고
    • Microbicides - Aids to safer sex
    • Shattock, R. Solomon, S. (2004) Microbicides - aids to safer sex. Lancet, 363, 1002 1003.
    • (2004) Lancet , vol.363 , pp. 1002-1003
    • Shattock, R.1    Solomon, S.2
  • 54
    • 0029685190 scopus 로고    scopus 로고
    • Protein extraction from plant tissues
    • In: Doonan, S., ed.), pp. Totawa, NJ: Humana Press.
    • Shewry, P.R. Fido, R.J. (1996) Protein extraction from plant tissues. In : Methods in Molecular Biology (Doonan, S., ed.), pp. 23 29. Totawa, NJ : Humana Press.
    • (1996) Methods in Molecular Biology , pp. 23-29
    • Shewry, P.R.1    Fido, R.J.2
  • 55
    • 0024728961 scopus 로고
    • Characterisation of monoclonal antibodies to common protein epitopes on the cell surface of Streptococcus mutans and Streptococcus sobrinus
    • Smith, R. Lehner, T. (1989) Characterisation of monoclonal antibodies to common protein epitopes on the cell surface of Streptococcus mutans and Streptococcus sobrinus. Oral Microbiol. Immunol. 4, 153 158.
    • (1989) Oral Microbiol. Immunol. , vol.4 , pp. 153-158
    • Smith, R.1    Lehner, T.2
  • 57
    • 33947321425 scopus 로고    scopus 로고
    • Pharma-Planta: Road testing the developing regulatory guidelines for plant-made pharmaceuticals
    • Sparrow, P.A.C., Irwin, J.A., Dale, P.J., Twyman, R.M. Ma, J.K.-C. (2007) Pharma-Planta: Road testing the developing regulatory guidelines for plant-made pharmaceuticals. Transgenic Res. 16, 147 161.
    • (2007) Transgenic Res. , vol.16 , pp. 147-161
    • Sparrow, P.A.C.1    Irwin, J.A.2    Dale, P.J.3    Twyman, R.M.4    Ma, J.K.-C.5
  • 58
    • 0026644802 scopus 로고
    • Retention of a type I1 surface membrane protein in the endoplasmic reticulum by the Lys-Asp-Glu-Leu sequence
    • Tang, B.L., Wong, S.H., Low, S.H. Hong, W. (1992) Retention of a type I1 surface membrane protein in the endoplasmic reticulum by the Lys-Asp-Glu-Leu sequence. J. Biol. Chem. 267, 7072 7076.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7072-7076
    • Tang, B.L.1    Wong, S.H.2    Low, S.H.3    Hong, W.4
  • 59
    • 0018599354 scopus 로고
    • Action of shear on enzymes: Studies with alcohol dehydrogenase
    • Thomas, C.R., Nienow, A.W. Dunnill, P. (1979) Action of shear on enzymes: studies with alcohol dehydrogenase. Biotechnol. Bioeng. 21, 2263 2278.
    • (1979) Biotechnol. Bioeng. , vol.21 , pp. 2263-2278
    • Thomas, C.R.1    Nienow, A.W.2    Dunnill, P.3
  • 60
    • 13844298876 scopus 로고    scopus 로고
    • Study on tobacco components involved in the pyrolytic generation of selected smoke constituents
    • Torikaiu, K., Uwano, Y., Nakamori, T., Tarora, W. Takahashi, H. (2005) Study on tobacco components involved in the pyrolytic generation of selected smoke constituents. Food Chem. Toxicol. 43, 559 568.
    • (2005) Food Chem. Toxicol. , vol.43 , pp. 559-568
    • Torikaiu, K.1    Uwano, Y.2    Nakamori, T.3    Tarora, W.4    Takahashi, H.5
  • 62
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer, A.W.P. Norde, W. (2000) The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys. J. 78, 394 404.
    • (2000) Biophys. J. , vol.78 , pp. 394-404
    • Vermeer, A.W.P.1    Norde, W.2
  • 63
    • 0035091578 scopus 로고    scopus 로고
    • Assembly and plasma membrane targeting of recombinant immunoglobulin chains in plants with a murine immunoglobulin transmembrane sequence
    • Vine, D.V., Drake, P., Hiatt, A. Ma, J.K.-C. (2001) Assembly and plasma membrane targeting of recombinant immunoglobulin chains in plants with a murine immunoglobulin transmembrane sequence. Plant Mol. Biol. 45, 159 167.
    • (2001) Plant Mol. Biol. , vol.45 , pp. 159-167
    • Vine, D.V.1    Drake, P.2    Hiatt, A.3    Ma, J.K.-C.4
  • 64
    • 0000870728 scopus 로고
    • Studies of the effects of shear on globular proteins. Extension to high shear fields and to pumps
    • Virkar, P.D., Narendranathan, T.J., Hoare, M. Dunnill, P. (1981) Studies of the effects of shear on globular proteins. Extension to high shear fields and to pumps. Biotechnol. Bioeng. 23, 425 429.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 425-429
    • Virkar, P.D.1    Narendranathan, T.J.2    Hoare, M.3    Dunnill, P.4
  • 65
    • 0031809410 scopus 로고    scopus 로고
    • Concanavalin a binding and endoglycosidase D resistance of β1,2-xylosylated and α1,3-fucosylated plant and insect oligosaccharides
    • Wilson, I.B.H. Altmann, F. (1998) Concanavalin A binding and endoglycosidase D resistance of β1,2-xylosylated and α1,3-fucosylated plant and insect oligosaccharides. Glycoconj. J. 15, 203 206.
    • (1998) Glycoconj. J. , vol.15 , pp. 203-206
    • Wilson, I.B.H.1    Altmann, F.2
  • 66
    • 0036061606 scopus 로고    scopus 로고
    • Removal of phenolic compounds in the production of high-quality canola protein isolates
    • Xu, L. Diosady, L.L. (2002) Removal of phenolic compounds in the production of high-quality canola protein isolates. Food Res. Int. 35, 23 30.
    • (2002) Food Res. Int. , vol.35 , pp. 23-30
    • Xu, L.1    Diosady, L.L.2
  • 68
    • 0035126481 scopus 로고    scopus 로고
    • Genetic engineering strategies for purification of recombinant proteins from canola by anion chromatography: An example of β-glucuronidase
    • Zhang, C., Love, R.T., Jilka, J.M. Glatz, C.E. (2001) Genetic engineering strategies for purification of recombinant proteins from canola by anion chromatography: an example of β-glucuronidase. Biotechnol. Prog. 17, 161 167.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 161-167
    • Zhang, C.1    Love, R.T.2    Jilka, J.M.3    Glatz, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.