메뉴 건너뛰기




Volumn 11, Issue 4, 2016, Pages 542-553

Enhanced GAD65 production in plants using the MagnICON transient expression system: Optimization of upstream production and downstream processing

Author keywords

Molecular farming; Protein engineering; Protein purification; Protein solubility; Type 1 diabetes

Indexed keywords

AMINO ACIDS; CYTOLOGY; PRODUCTION PLATFORMS; PROTEINS; PURIFICATION; SOLUBILITY; VACCINES;

EID: 84963542437     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201500187     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 84876576065 scopus 로고    scopus 로고
    • First plant-made biologic approved
    • Fox, J. L., First plant-made biologic approved. Nat. Biotechnol. 2012, 30, 472.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 472
    • Fox, J.L.1
  • 2
    • 84897553272 scopus 로고    scopus 로고
    • Comparative evaluation of recombinant protein production in different biofactories: The green perspectives
    • Merlin, M., Gecchele, E., Capaldi, S., Pezzotti, M., Avesani, L., Comparative evaluation of recombinant protein production in different biofactories: The green perspectives. Biomed. Res. Int. 2014, 2014, 136419.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 136419
    • Merlin, M.1    Gecchele, E.2    Capaldi, S.3    Pezzotti, M.4    Avesani, L.5
  • 3
    • 84895780170 scopus 로고    scopus 로고
    • Diabetes in the young - a global view and worldwide estimates of numbers of children with type 1 diabetes
    • Patterson, C., Guariguata, L., Dahlquist, G., Soltész, G. et al., Diabetes in the young - a global view and worldwide estimates of numbers of children with type 1 diabetes. Diabetes Res. Clin. Pract. 2014, 103, 161-175.
    • (2014) Diabetes Res. Clin. Pract. , vol.103 , pp. 161-175
    • Patterson, C.1    Guariguata, L.2    Dahlquist, G.3    Soltész, G.4
  • 4
    • 84963597200 scopus 로고    scopus 로고
    • Update on treatment of type 1 diabetes in childhood
    • Ludvigsson, J., Update on treatment of type 1 diabetes in childhood. Curr. Pediatr. Rep. 2013, 1, 118-127.
    • (2013) Curr. Pediatr. Rep. , vol.1 , pp. 118-127
    • Ludvigsson, J.1
  • 5
    • 84899627542 scopus 로고    scopus 로고
    • Comparative analysis of different biofactories for the production of a major diabetes autoantigen
    • Avesani, L., Merlin, M., Gecchele, E., Capaldi, S. et al., Comparative analysis of different biofactories for the production of a major diabetes autoantigen. Transgenic Res. 2014, 23, 281-291.
    • (2014) Transgenic Res. , vol.23 , pp. 281-291
    • Avesani, L.1    Merlin, M.2    Gecchele, E.3    Capaldi, S.4
  • 6
    • 84869012692 scopus 로고    scopus 로고
    • High-level transient expression of ER-targeted human interleukin 6 in Nicotiana benthamiana
    • Nausch, H., Mikschofsky, H., Koslowski, R., Meyer, U. et al., High-level transient expression of ER-targeted human interleukin 6 in Nicotiana benthamiana. PLoS ONE 2012, 7, e48938.
    • (2012) PLoS ONE , vol.7 , pp. e48938
    • Nausch, H.1    Mikschofsky, H.2    Koslowski, R.3    Meyer, U.4
  • 7
    • 0037144809 scopus 로고    scopus 로고
    • A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GD65
    • Kanaani, J., El-Husseini, A. E., Aguilera-Moreno, A., Diacovo, M. J. et al., A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GD65. J. Cell Biol. 2002, 158, 1229-1238.
    • (2002) J. Cell Biol. , vol.158 , pp. 1229-1238
    • Kanaani, J.1    El-Husseini, A.E.2    Aguilera-Moreno, A.3    Diacovo, M.J.4
  • 8
    • 0026690837 scopus 로고
    • Membrane anchoring of the autoantigen GAD65 to macrovesicles in pancreatic β-cells by palmitoylation in the N-terminal domain
    • Christgau, S., Aanstoot, H. J., Shierbeck, H., Begley, K. et al., Membrane anchoring of the autoantigen GAD65 to macrovesicles in pancreatic β-cells by palmitoylation in the N-terminal domain. J. Cell Biol. 1992, 118, 309-320.
    • (1992) J. Cell Biol. , vol.118 , pp. 309-320
    • Christgau, S.1    Aanstoot, H.J.2    Shierbeck, H.3    Begley, K.4
  • 9
    • 0028216264 scopus 로고
    • Amino acid residues 24-31 but not palmitoylation of cysteines 30 and 45 are requires for membrane anchoring of glutamic acid decarboxylase, GAD65
    • Shi, Y., Veit, B., Baekkeskov, S., Amino acid residues 24-31 but not palmitoylation of cysteines 30 and 45 are requires for membrane anchoring of glutamic acid decarboxylase, GAD65. J. Cell Biol. 1994, 124, 927-934.
    • (1994) J. Cell Biol. , vol.124 , pp. 927-934
    • Shi, Y.1    Veit, B.2    Baekkeskov, S.3
  • 10
    • 0033452018 scopus 로고    scopus 로고
    • Transgenic plants expressing human glutamic acid decarboxylase (GAD65), a major autoantigen in insulin-dependent diabetes mellitus
    • Porceddu, A., Falorni, A., Ferradini, N., Cosentino, A. et al., Transgenic plants expressing human glutamic acid decarboxylase (GAD65), a major autoantigen in insulin-dependent diabetes mellitus. Mol. Breed. 1999, 5, 553-560.
    • (1999) Mol. Breed. , vol.5 , pp. 553-560
    • Porceddu, A.1    Falorni, A.2    Ferradini, N.3    Cosentino, A.4
  • 11
    • 84899621687 scopus 로고    scopus 로고
    • A downstream process allowing the efficient isolation of a recombinant amphiphilic protein from tobacco leaves
    • Gecchele, E., Schillberg, S., Merlin, M., Pezzotti, M., Avesani, L., A downstream process allowing the efficient isolation of a recombinant amphiphilic protein from tobacco leaves. J. Chromatogr. B 2014, 960, 34-42.
    • (2014) J. Chromatogr. B , vol.960 , pp. 34-42
    • Gecchele, E.1    Schillberg, S.2    Merlin, M.3    Pezzotti, M.4    Avesani, L.5
  • 12
    • 0038056326 scopus 로고    scopus 로고
    • Improved in planta expression of the human islet autoantigen glutamic acid decarboxylase (GAD65)
    • Avesani, L., Falorni, A., Tornielli, G. B., Marusic, C. et al., Improved in planta expression of the human islet autoantigen glutamic acid decarboxylase (GAD65). Transgenic Res. 2003, 12, 203-212.
    • (2003) Transgenic Res. , vol.12 , pp. 203-212
    • Avesani, L.1    Falorni, A.2    Tornielli, G.B.3    Marusic, C.4
  • 13
    • 77955258362 scopus 로고    scopus 로고
    • Recombinant human GAD65 accumulates to high levels in transgenic tobacco plants when expressed as an enzymatically inactive mutant
    • Avesani, L., Vitale, A., Pedrazzini, E., deVirgilio, M. et al., Recombinant human GAD65 accumulates to high levels in transgenic tobacco plants when expressed as an enzymatically inactive mutant. Plant Biotechnol. J. 2010, 8, 862-872.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 862-872
    • Avesani, L.1    Vitale, A.2    Pedrazzini, E.3    deVirgilio, M.4
  • 14
    • 84919392745 scopus 로고    scopus 로고
    • Characterization of continuous B-cell epitopes in the N-terminus of glutamate decarboxylase67 using monoclonal antibodies
    • Agca, S., Houen, G., Trier, N. H., Characterization of continuous B-cell epitopes in the N-terminus of glutamate decarboxylase67 using monoclonal antibodies. J. Pept. Sci. 2014, 20, 928-934.
    • (2014) J. Pept. Sci. , vol.20 , pp. 928-934
    • Agca, S.1    Houen, G.2    Trier, N.H.3
  • 15
    • 48449102723 scopus 로고    scopus 로고
    • COOH-terminal clustering of autoantibody and T-cell determinants on the structure of GAD65 provide insights into the molecular basis of autoreactivity
    • Fenalti, G., Hampe, C. S., Arafat, Y., Law, R. H. et al., COOH-terminal clustering of autoantibody and T-cell determinants on the structure of GAD65 provide insights into the molecular basis of autoreactivity. Diabetes 2008, 57, 1293-1301.
    • (2008) Diabetes , vol.57 , pp. 1293-1301
    • Fenalti, G.1    Hampe, C.S.2    Arafat, Y.3    Law, R.H.4
  • 16
    • 0242362721 scopus 로고    scopus 로고
    • Identification and functional analysis of truncated human glutamic acid decarboxylase 65
    • Wei, J., Jin, Y., Wu, H., Sha, Di, Wu, J.-Y., Identification and functional analysis of truncated human glutamic acid decarboxylase 65. J. Biomed. Sci. 2003, 10, 617-624.
    • (2003) J. Biomed. Sci. , vol.10 , pp. 617-624
    • Wei, J.1    Jin, Y.2    Wu, H.3    Sha, D.4    Wu, J.-Y.5
  • 17
    • 34247249781 scopus 로고    scopus 로고
    • GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop
    • Fenalti, G., Law, R. H. P., Buckle, A. M., Langendorf, C., et al., GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat. Struct. Mol. Biol. 2007, 14, 280-286.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 280-286
    • Fenalti, G.1    Law, R.H.P.2    Buckle, A.M.3    Langendorf, C.4
  • 18
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY vectors for Agrobacterium-mediated plant transformation
    • Karimi, M., Inzè, D., Depicker, A., GATEWAY vectors for Agrobacterium-mediated plant transformation. Trends Plant Sci. 2002, 7, 193-195.
    • (2002) Trends Plant Sci. , vol.7 , pp. 193-195
    • Karimi, M.1    Inzè, D.2    Depicker, A.3
  • 19
    • 56649114274 scopus 로고    scopus 로고
    • A one spot, one step, precision cloning method with high throughput capability
    • Engler, C., Kandzia, R., Marillonnet, S., A one spot, one step, precision cloning method with high throughput capability. PLoS ONE 2008, 3, e3647.
    • (2008) PLoS ONE , vol.3 , pp. e3647
    • Engler, C.1    Kandzia, R.2    Marillonnet, S.3
  • 20
    • 84941236302 scopus 로고    scopus 로고
    • A comparative analysis of recombinant protein expression in different biofactories: Bacteria, insect cells and plant systems
    • Gecchele, E., Merlin, M., Brozzetti, A., Falorni, A., et al., A comparative analysis of recombinant protein expression in different biofactories: Bacteria, insect cells and plant systems. J. Visualized Exp. 2015, 97, e52459.
    • (2015) J. Visualized Exp. , vol.97 , pp. e52459
    • Gecchele, E.1    Merlin, M.2    Brozzetti, A.3    Falorni, A.4
  • 21
    • 0022550680 scopus 로고
    • Analysis of Agrobacterium tumefaciens virulence mutants in leaf discs
    • Horsch, R. B., Klee, H. J., Stachel, S., Winans, S. C. et al., Analysis of Agrobacterium tumefaciens virulence mutants in leaf discs. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 2571-2575.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2571-2575
    • Horsch, R.B.1    Klee, H.J.2    Stachel, S.3    Winans, S.C.4
  • 22
    • 16544390244 scopus 로고    scopus 로고
    • Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm
    • Arcalis, E., Marcel, S., Altmann, F., Kolarich, D. et al., Unexpected deposition patterns of recombinant proteins in post-endoplasmic reticulum compartments of wheat endosperm. Plant Physiol. 2004, 136, 3457-3466.
    • (2004) Plant Physiol. , vol.136 , pp. 3457-3466
    • Arcalis, E.1    Marcel, S.2    Altmann, F.3    Kolarich, D.4
  • 23
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., Flügge, U. I., A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 1984, 138, 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 24
    • 4444354996 scopus 로고    scopus 로고
    • New protamine quantification method in microtiter plates using o-phthaldialdehyde/N-acetyl-L-cysteine reagent
    • Lochmann, D., Stadlhofer, S., Weyermann, J., Zimmer, A., New protamine quantification method in microtiter plates using o-phthaldialdehyde/N-acetyl-L-cysteine reagent. Int. J. Pharm. 2004, 283, 11-17.
    • (2004) Int. J. Pharm. , vol.283 , pp. 11-17
    • Lochmann, D.1    Stadlhofer, S.2    Weyermann, J.3    Zimmer, A.4
  • 25
    • 0000359845 scopus 로고
    • Colorimetry of total phenolics with phosphomolybdic-phosphotungstic acid reagents
    • Singleton, V. L., Rossi, J. A., Colorimetry of total phenolics with phosphomolybdic-phosphotungstic acid reagents. Am. J. Enol. Vitic. 1965, 16, 144-158.
    • (1965) Am. J. Enol. Vitic. , vol.16 , pp. 144-158
    • Singleton, V.L.1    Rossi, J.A.2
  • 26
    • 2342525801 scopus 로고    scopus 로고
    • In planta engineering of viral RNA replicons: Efficient assembly by recombination of DNA modules delivered by Agrobacterium
    • Marillonnet, S., Giritch, A., Gils, M., Kandzia, R. et al., In planta engineering of viral RNA replicons: Efficient assembly by recombination of DNA modules delivered by Agrobacterium. Proc. Natl. Acad. Sci. USA 2004, 101, 6852-6857.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6852-6857
    • Marillonnet, S.1    Giritch, A.2    Gils, M.3    Kandzia, R.4
  • 27
    • 78751476705 scopus 로고    scopus 로고
    • Site-specific analysis of protein S-acylation by resin-assisted capture
    • Forrester, M. T., Hess, D. T., Thompson, J. W., Hultman, R. et al., Site-specific analysis of protein S-acylation by resin-assisted capture. J. Lipid Res. 2011, 52, 393-398.
    • (2011) J. Lipid Res. , vol.52 , pp. 393-398
    • Forrester, M.T.1    Hess, D.T.2    Thompson, J.W.3    Hultman, R.4
  • 28
    • 79953885738 scopus 로고    scopus 로고
    • Phenolics removal from transgenic Lemna minor extracts expressing mAb and impact on mAb production cost
    • Barros, G. O., Woodard, S. L., Nikolov, Z. L., Phenolics removal from transgenic Lemna minor extracts expressing mAb and impact on mAb production cost. Biotechnol. Prog. 2011, 27, 410-418.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 410-418
    • Barros, G.O.1    Woodard, S.L.2    Nikolov, Z.L.3
  • 29
    • 4043094059 scopus 로고    scopus 로고
    • Considerations for the recovery of recombinant proteins from plants
    • Menkhaus, T. J., Bai, Y., Zhang, C., Nikolov, Z. L., Glatz, C. E., Considerations for the recovery of recombinant proteins from plants. Biotechnol. Prog. 2004, 20, 1001-1014.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 1001-1014
    • Menkhaus, T.J.1    Bai, Y.2    Zhang, C.3    Nikolov, Z.L.4    Glatz, C.E.5
  • 30
    • 33947161574 scopus 로고    scopus 로고
    • A robust purification strategy to accelerate membrane proteomics
    • Dobrovetsky, E., Menendez, J., Edwards, A. M., Koth, C. M., A robust purification strategy to accelerate membrane proteomics. Methods 2007, 41, 381-387.
    • (2007) Methods , vol.41 , pp. 381-387
    • Dobrovetsky, E.1    Menendez, J.2    Edwards, A.M.3    Koth, C.M.4
  • 31
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener, M. C., A pedestrian guide to membrane protein crystallization. Methods 2004, 34, 364-372.
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 32
    • 84859726807 scopus 로고    scopus 로고
    • Interference of some aqueous two-phase system phase-forming components in protein determination by the Bradford method
    • Silverio, S. C., Moreira, S., Milagres, A. M. F., Macedo, E. A. et al., Interference of some aqueous two-phase system phase-forming components in protein determination by the Bradford method. Anal. Biochem. 2012, 421, 719-724.
    • (2012) Anal. Biochem. , vol.421 , pp. 719-724
    • Silverio, S.C.1    Moreira, S.2    Milagres, A.M.F.3    Macedo, E.A.4
  • 33
    • 79959725932 scopus 로고    scopus 로고
    • Efficient removal of detergents from proteins and peptides in a spin column format
    • Antharavally, B. S., Mallia, K. A., Rosenblatt, M. M., Salunkhe, A. M. et al., Efficient removal of detergents from proteins and peptides in a spin column format. Anal. Biochem. 2011, 416, 39-44.
    • (2011) Anal. Biochem. , vol.416 , pp. 39-44
    • Antharavally, B.S.1    Mallia, K.A.2    Rosenblatt, M.M.3    Salunkhe, A.M.4
  • 34
    • 84938229047 scopus 로고    scopus 로고
    • The removal of Triton X-100 by dialysis is feasible
    • Opitz, S., Hannika, F., Krüger, T., Rhode, H., The removal of Triton X-100 by dialysis is feasible. Anal. Bioanal. Chem. 2014, 407, 1107-1118.
    • (2014) Anal. Bioanal. Chem. , vol.407 , pp. 1107-1118
    • Opitz, S.1    Hannika, F.2    Krüger, T.3    Rhode, H.4
  • 35
    • 0000146626 scopus 로고    scopus 로고
    • An Agrobacterium-mediated transient gene expression system for intact leaves
    • Kapila, J., De Rycke, R., Van Montagu, M., Angenon, G., An Agrobacterium-mediated transient gene expression system for intact leaves. Plant Sci. 1997, 122, 101-108.
    • (1997) Plant Sci. , vol.122 , pp. 101-108
    • Kapila, J.1    De Rycke, R.2    Van Montagu, M.3    Angenon, G.4
  • 36
    • 0035983933 scopus 로고    scopus 로고
    • Targeting tryptophan decarboxylase to selected subcellular compartments of tobacco plants affects enzyme stability and in vivo function and leads to a lesion-mimic phenotype
    • Di Fiore, S., Li, Q., Leech, M. J., Schuster, F. et al., Targeting tryptophan decarboxylase to selected subcellular compartments of tobacco plants affects enzyme stability and in vivo function and leads to a lesion-mimic phenotype. Plant Physiol. 2002, 129, 1160-1169.
    • (2002) Plant Physiol. , vol.129 , pp. 1160-1169
    • Di Fiore, S.1    Li, Q.2    Leech, M.J.3    Schuster, F.4
  • 37
    • 84955199120 scopus 로고    scopus 로고
    • The rat ErbB2 tyrosine kinase receptor produced in plants is immunogenic in mice and confers protective immunity against ErbB2+ mammary cancer
    • Matić, S., Quaglino, E., Arata, L., Riccardo, F. et al., The rat ErbB2 tyrosine kinase receptor produced in plants is immunogenic in mice and confers protective immunity against ErbB2+ mammary cancer. Plant Biotechnol. J. 2015, 14, 153-159.
    • (2015) Plant Biotechnol. J. , vol.14 , pp. 153-159
    • Matić, S.1    Quaglino, E.2    Arata, L.3    Riccardo, F.4
  • 38
    • 0025718751 scopus 로고
    • Pancreatic beta cells express two autoantigenic forms of glutamic acid decarboxylase, a 65-kDa hydrophilic form and a 64-kDa amphiphilic form which can be both membrane-bound and soluble
    • Christgau, S., Schierbeck, H., Aanstoot, H. J., Aagaard, L. et al., Pancreatic beta cells express two autoantigenic forms of glutamic acid decarboxylase, a 65-kDa hydrophilic form and a 64-kDa amphiphilic form which can be both membrane-bound and soluble. J. Biol. Chem. 1991, 266, 21257-21264.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21257-21264
    • Christgau, S.1    Schierbeck, H.2    Aanstoot, H.J.3    Aagaard, L.4
  • 39
    • 77956383991 scopus 로고    scopus 로고
    • Two distinct mechanisms target GAD67 to vesicular pathways and presynaptic clusters
    • Kanaani, J., Kolibachuk, J., Martinez, H., Baekkeskov, S., Two distinct mechanisms target GAD67 to vesicular pathways and presynaptic clusters. J. Cell Biol. 2010, 190, 911-925.
    • (2010) J. Cell Biol. , vol.190 , pp. 911-925
    • Kanaani, J.1    Kolibachuk, J.2    Martinez, H.3    Baekkeskov, S.4
  • 40
    • 40949117546 scopus 로고    scopus 로고
    • A palmitoylation cycle dynamically regulates partitioning of the GABA-synthesizing enzyme GAD65 between ER-Golgi and post-Golgi membranes
    • Kanaani, J., Patterson, G., Schaufele, F., Lippincott-Schwartz, J., Baekkeskov, S., A palmitoylation cycle dynamically regulates partitioning of the GABA-synthesizing enzyme GAD65 between ER-Golgi and post-Golgi membranes. J. Cell Sci. 2008, 121, 437-449.
    • (2008) J. Cell Sci. , vol.121 , pp. 437-449
    • Kanaani, J.1    Patterson, G.2    Schaufele, F.3    Lippincott-Schwartz, J.4    Baekkeskov, S.5
  • 41
    • 61449113906 scopus 로고    scopus 로고
    • Protein S-acylation in plants
    • Hemsley, P. A., Protein S-acylation in plants. Mol. Membr. Biol. 2009, 26, 114-125.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 114-125
    • Hemsley, P.A.1
  • 42
    • 0032415715 scopus 로고    scopus 로고
    • Autoantigenic reactivity of diabetes sera with a hybrid glutamic acid decarboxylase GAD67-65 molecule GAD67(1-101)/GAD65(96-585)
    • Teoh, K. L., Fida, S., Rowley, M. J., Mackay, I. R., Autoantigenic reactivity of diabetes sera with a hybrid glutamic acid decarboxylase GAD67-65 molecule GAD67(1-101)/GAD65(96-585). Autoimmunity 1998, 28, 259-266.
    • (1998) Autoimmunity , vol.28 , pp. 259-266
    • Teoh, K.L.1    Fida, S.2    Rowley, M.J.3    Mackay, I.R.4
  • 43
    • 0032568191 scopus 로고    scopus 로고
    • Expression in Saccharomyces cerevisiae of antigenically and enzymatically active recombinant glutamic acid decarboxylase
    • Law, R. H. P., Rowley, M. J., Machay, I. R., Corner, B., Expression in Saccharomyces cerevisiae of antigenically and enzymatically active recombinant glutamic acid decarboxylase. J. Biotechnol. 1998, 61, 57-68.
    • (1998) J. Biotechnol. , vol.61 , pp. 57-68
    • Law, R.H.P.1    Rowley, M.J.2    Machay, I.R.3    Corner, B.4
  • 44
    • 0034212493 scopus 로고    scopus 로고
    • Comparative expression and purification of human glutamic acid decarboxylase from Saccharomyces cerevisiae and Pichia pastoris
    • Papakonstantinou, T., Law, R. H. P., Gardiner, P., Rowley, M. J., Mackay, I. R., Comparative expression and purification of human glutamic acid decarboxylase from Saccharomyces cerevisiae and Pichia pastoris. Enzyme Microb. Technol. 2000, 26, 645-652.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 645-652
    • Papakonstantinou, T.1    Law, R.H.P.2    Gardiner, P.3    Rowley, M.J.4    Mackay, I.R.5
  • 45
    • 79959701787 scopus 로고    scopus 로고
    • Non-food/feed seeds as biofactories for the high-yield production of recombinant pharmaceuticals
    • Morandini, F., Avesani, L., Bortesi, L., Van Droogenbroeck, B. et al., Non-food/feed seeds as biofactories for the high-yield production of recombinant pharmaceuticals. Plant Biotechnol. J. 2011, 9, 911-921.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 911-921
    • Morandini, F.1    Avesani, L.2    Bortesi, L.3    Van Droogenbroeck, B.4
  • 46
    • 45149131892 scopus 로고    scopus 로고
    • Advances in primary recovery: Centrifugation and membrane technology
    • Roush, D. J., Lu, Y., Advances in primary recovery: Centrifugation and membrane technology. Biotechnol. Prog. 2008, 24, 488-495.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 488-495
    • Roush, D.J.1    Lu, Y.2
  • 47
    • 0024716141 scopus 로고
    • Purification technologies for plant proteins
    • Jervis, L., Pierpoint, W. S., Purification technologies for plant proteins. J. Biotechnol. 1989, 11, 161-198.
    • (1989) J. Biotechnol. , vol.11 , pp. 161-198
    • Jervis, L.1    Pierpoint, W.S.2
  • 48
    • 70349333751 scopus 로고    scopus 로고
    • Evaluation of monoclonal antibody and phenolic extraction from transgenic Lemna for purification process development
    • Woodard, S. L., Wilken, L. R., Barros, G. O., White, S. G, Nikolov, Z. L., Evaluation of monoclonal antibody and phenolic extraction from transgenic Lemna for purification process development. Biotechnol. Bioeng. 2009, 104, 562-571.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 562-571
    • Woodard, S.L.1    Wilken, L.R.2    Barros, G.O.3    White, S.G.4    Nikolov, Z.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.