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Volumn 26, Issue 9, 2008, Pages 518-525

Affinity chromatography approaches to overcome the challenges of purifying plasmid DNA

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHROMATOGRAPHIC ANALYSIS; CHROMATOGRAPHY; DNA; GENES; MOLECULAR BIOLOGY; NUCLEIC ACIDS; ORGANIC ACIDS;

EID: 48849111296     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2008.05.005     Document Type: Review
Times cited : (108)

References (75)
  • 1
    • 34848903876 scopus 로고    scopus 로고
    • Plasmid DNA and viral vector-based vaccines for the treatment of cancer
    • Anderson R.J., and Schneider J. Plasmid DNA and viral vector-based vaccines for the treatment of cancer. Vaccine 25 Suppl. 2 (2007) B24-B34
    • (2007) Vaccine , vol.25 , Issue.SUPPL. 2
    • Anderson, R.J.1    Schneider, J.2
  • 2
    • 0033120652 scopus 로고    scopus 로고
    • Large-scale production of pharmaceutical-grade plasmid DNA for gene therapy: problems and bottlenecks
    • Prazeres D.M.F., et al. Large-scale production of pharmaceutical-grade plasmid DNA for gene therapy: problems and bottlenecks. Trends Biotechnol. 17 (1999) 169-174
    • (1999) Trends Biotechnol. , vol.17 , pp. 169-174
    • Prazeres, D.M.F.1
  • 3
    • 33847218598 scopus 로고    scopus 로고
    • Vaccine delivery methods using viral vectors
    • Brave A., et al. Vaccine delivery methods using viral vectors. Mol. Pharm. 4 (2007) 18-32
    • (2007) Mol. Pharm. , vol.4 , pp. 18-32
    • Brave, A.1
  • 4
    • 0032538597 scopus 로고    scopus 로고
    • Induction of antigen-specific cytotoxic T lymphocytes in humans by a malaria DNA vaccine
    • Wang R., et al. Induction of antigen-specific cytotoxic T lymphocytes in humans by a malaria DNA vaccine. Science 282 (1998) 476-480
    • (1998) Science , vol.282 , pp. 476-480
    • Wang, R.1
  • 5
    • 11144355460 scopus 로고    scopus 로고
    • A human immunodeficiency virus 1 (HIV-1) clade A vaccine in clinical trials: stimulation of HIV-specific T-cell responses by DNA and recombinant modified vaccinia virus Ankara (MVA) vaccines in humans
    • Mwau M., et al. A human immunodeficiency virus 1 (HIV-1) clade A vaccine in clinical trials: stimulation of HIV-specific T-cell responses by DNA and recombinant modified vaccinia virus Ankara (MVA) vaccines in humans. J. Gen. Virol. 85 (2004) 911-919
    • (2004) J. Gen. Virol. , vol.85 , pp. 911-919
    • Mwau, M.1
  • 6
    • 33846909686 scopus 로고    scopus 로고
    • A DNA vaccine for Ebola virus is safe and immunogenic in a phase I clinical trial
    • Martin J.E., et al. A DNA vaccine for Ebola virus is safe and immunogenic in a phase I clinical trial. Clin. Vaccine. Immunol. 13 (2006) 1267-1277
    • (2006) Clin. Vaccine. Immunol. , vol.13 , pp. 1267-1277
    • Martin, J.E.1
  • 7
    • 0033055999 scopus 로고    scopus 로고
    • DNA vaccine encoding hemagglutinin provides protective immunity against H5N1 influenza virus infection in mice
    • Kodihalli S., et al. DNA vaccine encoding hemagglutinin provides protective immunity against H5N1 influenza virus infection in mice. J. Virol. 73 (1999) 2094-2098
    • (1999) J. Virol. , vol.73 , pp. 2094-2098
    • Kodihalli, S.1
  • 8
    • 28844490036 scopus 로고    scopus 로고
    • Bioprocess engineering issues that would be faced in producing a DNA vaccine at up to 100 m3 fermentation scale for an influenza pandemic
    • Hoare M., et al. Bioprocess engineering issues that would be faced in producing a DNA vaccine at up to 100 m3 fermentation scale for an influenza pandemic. Biotechnol. Prog. 21 (2005) 1577-1592
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1577-1592
    • Hoare, M.1
  • 9
    • 0037664871 scopus 로고    scopus 로고
    • Phase I study of intranodal delivery of a plasmid DNA vaccine for patients with Stage IV melanoma
    • Tagawa S.T., et al. Phase I study of intranodal delivery of a plasmid DNA vaccine for patients with Stage IV melanoma. Cancer 98 (2003) 144-154
    • (2003) Cancer , vol.98 , pp. 144-154
    • Tagawa, S.T.1
  • 10
    • 3543025721 scopus 로고    scopus 로고
    • Safety evaluation of clinical gene therapy using hepatocyte growth factor to treat peripheral arterial disease
    • Morishita R., et al. Safety evaluation of clinical gene therapy using hepatocyte growth factor to treat peripheral arterial disease. Hypertension 44 (2004) 203-209
    • (2004) Hypertension , vol.44 , pp. 203-209
    • Morishita, R.1
  • 12
    • 3042667834 scopus 로고    scopus 로고
    • Animal-free production of ccc-supercoiled plasmids for research and clinical applications
    • Schleef M., and Schmidt T. Animal-free production of ccc-supercoiled plasmids for research and clinical applications. J. Gene Med. 6 (2004) S45-S53
    • (2004) J. Gene Med. , vol.6
    • Schleef, M.1    Schmidt, T.2
  • 14
    • 35748978569 scopus 로고    scopus 로고
    • Circular dichroism investigation of the effect of plasmid DNA structure on retention in histidine chromatography
    • Sousa F., et al. Circular dichroism investigation of the effect of plasmid DNA structure on retention in histidine chromatography. Arch. Biochem. Biophys. 467 (2007) 154-162
    • (2007) Arch. Biochem. Biophys. , vol.467 , pp. 154-162
    • Sousa, F.1
  • 15
    • 14244251286 scopus 로고    scopus 로고
    • Impact of plasmid supercoiling on the efficacy of a rabies DNA vaccine to protect cats
    • Cupillard L., et al. Impact of plasmid supercoiling on the efficacy of a rabies DNA vaccine to protect cats. Vaccine 23 (2005) 1910-1916
    • (2005) Vaccine , vol.23 , pp. 1910-1916
    • Cupillard, L.1
  • 16
    • 0032790308 scopus 로고    scopus 로고
    • Effect of DNA topology on the transfection efficiency of poly((2-dimethylamino)ethyl methacrylate)-plasmid complexes
    • Cherng J.Y., et al. Effect of DNA topology on the transfection efficiency of poly((2-dimethylamino)ethyl methacrylate)-plasmid complexes. J. Control. Release 60 (1999) 343-353
    • (1999) J. Control. Release , vol.60 , pp. 343-353
    • Cherng, J.Y.1
  • 17
    • 4644359883 scopus 로고    scopus 로고
    • Plasmid DNA purification
    • Stadler J., et al. Plasmid DNA purification. J. Gene Med. 6 (2004) S54-S66
    • (2004) J. Gene Med. , vol.6
    • Stadler, J.1
  • 18
    • 15244358693 scopus 로고    scopus 로고
    • Chromatography of plasmid DNA
    • Diogo M.M., et al. Chromatography of plasmid DNA. J. Chromatogr. A. 1069 (2005) 3-22
    • (2005) J. Chromatogr. A. , vol.1069 , pp. 3-22
    • Diogo, M.M.1
  • 19
    • 0034284422 scopus 로고    scopus 로고
    • Downstream processing of plasmid DNA for gene therapy and DNA vaccine applications
    • Ferreira G.N., et al. Downstream processing of plasmid DNA for gene therapy and DNA vaccine applications. Trends Biotechnol. 18 (2000) 380-388
    • (2000) Trends Biotechnol. , vol.18 , pp. 380-388
    • Ferreira, G.N.1
  • 20
    • 0033167256 scopus 로고    scopus 로고
    • Development of process flow sheets for the purification of supercoiled plasmids for gene therapy applications
    • Ferreira G.N., et al. Development of process flow sheets for the purification of supercoiled plasmids for gene therapy applications. Biotechnol. Prog. 15 (1999) 725-731
    • (1999) Biotechnol. Prog. , vol.15 , pp. 725-731
    • Ferreira, G.N.1
  • 21
    • 34249748433 scopus 로고    scopus 로고
    • Studies on endotoxin removal mechanism of adsorbents with amino acid ligands
    • Wei Z., et al. Studies on endotoxin removal mechanism of adsorbents with amino acid ligands. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 852 (2007) 288-292
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.852 , pp. 288-292
    • Wei, Z.1
  • 22
    • 39549086017 scopus 로고    scopus 로고
    • Prediction of diffusion coefficients of plasmids
    • Prazeres D.M.F. Prediction of diffusion coefficients of plasmids. Biotechnol. Bioeng. 99 (2008) 1040-1044
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 1040-1044
    • Prazeres, D.M.F.1
  • 23
    • 33845426368 scopus 로고    scopus 로고
    • Superporous agarose anion exchangers for plasmid isolation
    • Tiainen P., et al. Superporous agarose anion exchangers for plasmid isolation. J. Chromatogr. A. 1138 (2007) 84-94
    • (2007) J. Chromatogr. A. , vol.1138 , pp. 84-94
    • Tiainen, P.1
  • 24
    • 0032969578 scopus 로고    scopus 로고
    • Continuous superporous agarose beds for chromatography and electrophoresis
    • Gustavsson P.E., and Larsson P.O. Continuous superporous agarose beds for chromatography and electrophoresis. J. Chromatogr. A. 832 (1999) 29-39
    • (1999) J. Chromatogr. A. , vol.832 , pp. 29-39
    • Gustavsson, P.E.1    Larsson, P.O.2
  • 25
    • 4344612043 scopus 로고    scopus 로고
    • Characterization of methacrylate monoliths for purification of DNA molecules
    • Bencina M., et al. Characterization of methacrylate monoliths for purification of DNA molecules. J. Sep. Sci. 27 (2004) 801-810
    • (2004) J. Sep. Sci. , vol.27 , pp. 801-810
    • Bencina, M.1
  • 26
    • 1642441457 scopus 로고    scopus 로고
    • Application of short monolithic columns for fast purification of plasmid DNA
    • Branovic K., et al. Application of short monolithic columns for fast purification of plasmid DNA. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 801 (2004) 331-337
    • (2004) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.801 , pp. 331-337
    • Branovic, K.1
  • 27
    • 4344678036 scopus 로고    scopus 로고
    • Monoliths for fast bioseparation and bioconversion and their applications in biotechnology
    • Jungbauer A., and Hahn R. Monoliths for fast bioseparation and bioconversion and their applications in biotechnology. J. Sep. Sci. 27 (2004) 767-778
    • (2004) J. Sep. Sci. , vol.27 , pp. 767-778
    • Jungbauer, A.1    Hahn, R.2
  • 28
    • 13844254962 scopus 로고    scopus 로고
    • Application of monoliths for plasmid DNA purification development and transfer to production
    • Urthaler J., et al. Application of monoliths for plasmid DNA purification development and transfer to production. J. Chromatogr. A. 1065 (2005) 93-106
    • (2005) J. Chromatogr. A. , vol.1065 , pp. 93-106
    • Urthaler, J.1
  • 29
    • 0032528715 scopus 로고    scopus 로고
    • High-performance membrane chromatography of supercoiled plasmid DNA
    • Giovannini R., et al. High-performance membrane chromatography of supercoiled plasmid DNA. Anal. Chem. 70 (1998) 3348-3354
    • (1998) Anal. Chem. , vol.70 , pp. 3348-3354
    • Giovannini, R.1
  • 30
    • 0037424580 scopus 로고    scopus 로고
    • Adsorptive membrane chromatography for purification of plasmid DNA
    • Teeters M.A., et al. Adsorptive membrane chromatography for purification of plasmid DNA. J. Chromatogr. A. 989 (2003) 165-173
    • (2003) J. Chromatogr. A. , vol.989 , pp. 165-173
    • Teeters, M.A.1
  • 31
    • 33845674679 scopus 로고    scopus 로고
    • Effect of salt on purification of plasmid DNA using size-exclusion chromatography
    • Li L.Z., et al. Effect of salt on purification of plasmid DNA using size-exclusion chromatography. J. Chromatogr. A. 1139 (2007) 228-235
    • (2007) J. Chromatogr. A. , vol.1139 , pp. 228-235
    • Li, L.Z.1
  • 32
    • 0032496250 scopus 로고    scopus 로고
    • Preparative purification of supercoiled plasmid DNA using anion-exchange chromatography
    • Prazeres D.M.F., et al. Preparative purification of supercoiled plasmid DNA using anion-exchange chromatography. J. Chromatogr. A. 806 (1998) 31-45
    • (1998) J. Chromatogr. A. , vol.806 , pp. 31-45
    • Prazeres, D.M.F.1
  • 33
    • 1842787939 scopus 로고    scopus 로고
    • Purification of pharmaceutical-grade plasmid DNA by anion-exchange chromatography in an RNase-free process
    • Eon-Duval A., and Burke G. Purification of pharmaceutical-grade plasmid DNA by anion-exchange chromatography in an RNase-free process. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 804 (2004) 327-335
    • (2004) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.804 , pp. 327-335
    • Eon-Duval, A.1    Burke, G.2
  • 34
    • 0030570998 scopus 로고    scopus 로고
    • Sequence-dependent DNA separation by anion-exchange high-performance liquid chromatography
    • Yamakawa H., et al. Sequence-dependent DNA separation by anion-exchange high-performance liquid chromatography. Anal. Biochem. 240 (1996) 242-250
    • (1996) Anal. Biochem. , vol.240 , pp. 242-250
    • Yamakawa, H.1
  • 35
    • 0032496180 scopus 로고    scopus 로고
    • Micropellicular stationary phases for high-performance liquid chromatography of double-stranded DNA
    • Huber C.G. Micropellicular stationary phases for high-performance liquid chromatography of double-stranded DNA. J. Chromatogr. A. 806 (1998) 3-30
    • (1998) J. Chromatogr. A. , vol.806 , pp. 3-30
    • Huber, C.G.1
  • 36
    • 34250767811 scopus 로고    scopus 로고
    • Generalizing a two-conformation model for describing salt and temperature effects on protein retention and stability in hydrophobic interaction chromatography
    • Xiao Y., et al. Generalizing a two-conformation model for describing salt and temperature effects on protein retention and stability in hydrophobic interaction chromatography. J. Chromatogr. A. 1157 (2007) 197-206
    • (2007) J. Chromatogr. A. , vol.1157 , pp. 197-206
    • Xiao, Y.1
  • 37
    • 20444483268 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins. III. Unfolding of proteins upon adsorption
    • Jungbauer A., et al. Hydrophobic interaction chromatography of proteins. III. Unfolding of proteins upon adsorption. J. Chromatogr. A. 1079 (2005) 221-228
    • (2005) J. Chromatogr. A. , vol.1079 , pp. 221-228
    • Jungbauer, A.1
  • 38
    • 0037183740 scopus 로고    scopus 로고
    • Rapid analysis of a plasmid by hydrophobic-interaction chromatography with a non-porous resin
    • Iuliano S., et al. Rapid analysis of a plasmid by hydrophobic-interaction chromatography with a non-porous resin. J. Chromatogr. A. 972 (2002) 77-86
    • (2002) J. Chromatogr. A. , vol.972 , pp. 77-86
    • Iuliano, S.1
  • 39
    • 0035554023 scopus 로고    scopus 로고
    • Studies on the retention of plasmid DNA and Escherichia coli nucleic acids by hydrophobic interaction chromatography
    • Diogo M.M., et al. Studies on the retention of plasmid DNA and Escherichia coli nucleic acids by hydrophobic interaction chromatography. Bioseparation 10 (2001) 211-220
    • (2001) Bioseparation , vol.10 , pp. 211-220
    • Diogo, M.M.1
  • 40
    • 0034608587 scopus 로고    scopus 로고
    • Purification of a cystic fibrosis plasmid vector for gene therapy using hydrophobic interaction chromatography
    • Diogo M.M., et al. Purification of a cystic fibrosis plasmid vector for gene therapy using hydrophobic interaction chromatography. Biotechnol. Bioeng. 68 (2000) 576-583
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 576-583
    • Diogo, M.M.1
  • 41
    • 0035523565 scopus 로고    scopus 로고
    • Production, purification and analysis of an experimental DNA vaccine against rabies
    • Diogo M.M., et al. Production, purification and analysis of an experimental DNA vaccine against rabies. J. Gene Med. 3 (2001) 577-584
    • (2001) J. Gene Med. , vol.3 , pp. 577-584
    • Diogo, M.M.1
  • 42
    • 0038392599 scopus 로고    scopus 로고
    • Assessment of purity and quantification of plasmid DNA in process solutions using high-performance hydrophobic interaction chromatography
    • Diogo M.M., et al. Assessment of purity and quantification of plasmid DNA in process solutions using high-performance hydrophobic interaction chromatography. J. Chromatogr. A. 998 (2003) 109-117
    • (2003) J. Chromatogr. A. , vol.998 , pp. 109-117
    • Diogo, M.M.1
  • 43
    • 0030968156 scopus 로고    scopus 로고
    • A comparison of gel filtration chromatographic supports for plasmid purification
    • Ferreira G.N., et al. A comparison of gel filtration chromatographic supports for plasmid purification. Biotechnol. Tech. 11 (1997) 417-420
    • (1997) Biotechnol. Tech. , vol.11 , pp. 417-420
    • Ferreira, G.N.1
  • 44
    • 0034080617 scopus 로고    scopus 로고
    • Studies on the batch adsorption of plasmid DNA onto anion-exchange chromatographic supports
    • Ferreira G.N., et al. Studies on the batch adsorption of plasmid DNA onto anion-exchange chromatographic supports. Biotechnol. Prog. 16 (2000) 416-424
    • (2000) Biotechnol. Prog. , vol.16 , pp. 416-424
    • Ferreira, G.N.1
  • 45
    • 0032927212 scopus 로고    scopus 로고
    • Superporous agarose beads as a hydrophobic interaction chromatography support
    • Gustavsson P.E., et al. Superporous agarose beads as a hydrophobic interaction chromatography support. J. Chromatogr. A. 830 (1999) 275-284
    • (1999) J. Chromatogr. A. , vol.830 , pp. 275-284
    • Gustavsson, P.E.1
  • 46
    • 0037419671 scopus 로고    scopus 로고
    • Supercoiled plasmid DNA: selective purification by thiophilic/aromatic adsorption
    • Lemmens R., et al. Supercoiled plasmid DNA: selective purification by thiophilic/aromatic adsorption. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 784 (2003) 291-300
    • (2003) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.784 , pp. 291-300
    • Lemmens, R.1
  • 47
    • 0035975869 scopus 로고    scopus 로고
    • New developments in affinity chromatography with potential application in the production of biopharmaceuticals
    • Lowe C.R., et al. New developments in affinity chromatography with potential application in the production of biopharmaceuticals. J. Biochem. Biophys. Methods 49 (2001) 561-574
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 561-574
    • Lowe, C.R.1
  • 48
    • 0023046713 scopus 로고
    • New support for the large-scale purification of proteins
    • Kanoun S., et al. New support for the large-scale purification of proteins. J. Chromatogr. 376 (1986) 259-267
    • (1986) J. Chromatogr. , vol.376 , pp. 259-267
    • Kanoun, S.1
  • 49
    • 33646192500 scopus 로고    scopus 로고
    • Applications of silica supports in affinity chromatography
    • Schiel J.E., et al. Applications of silica supports in affinity chromatography. J. Sep. Sci. 29 (2006) 719-737
    • (2006) J. Sep. Sci. , vol.29 , pp. 719-737
    • Schiel, J.E.1
  • 50
    • 33645420958 scopus 로고    scopus 로고
    • The affinity concept in bioseparation: evolving paradigms and expanding range of applications
    • Mondal K., and Gupta M.N. The affinity concept in bioseparation: evolving paradigms and expanding range of applications. Biomol. Eng. 23 (2006) 59-76
    • (2006) Biomol. Eng. , vol.23 , pp. 59-76
    • Mondal, K.1    Gupta, M.N.2
  • 51
    • 33746941339 scopus 로고    scopus 로고
    • Design of a novel MEMS platform for the biaxial stimulation of living cells
    • Scuor N., et al. Design of a novel MEMS platform for the biaxial stimulation of living cells. Biomed. Microdevices 8 (2006) 239-246
    • (2006) Biomed. Microdevices , vol.8 , pp. 239-246
    • Scuor, N.1
  • 52
    • 40549114921 scopus 로고    scopus 로고
    • Nanoscaling laws of magnetic nanoparticles and their applicabilities in biomedical sciences
    • Jun Y.W., et al. Nanoscaling laws of magnetic nanoparticles and their applicabilities in biomedical sciences. Acc. Chem. Res. 41 (2008) 179-189
    • (2008) Acc. Chem. Res. , vol.41 , pp. 179-189
    • Jun, Y.W.1
  • 53
    • 33748418031 scopus 로고    scopus 로고
    • Affinity monolith chromatography
    • Mallik R., and Hage D.S. Affinity monolith chromatography. J. Sep. Sci. 29 (2006) 1686-1704
    • (2006) J. Sep. Sci. , vol.29 , pp. 1686-1704
    • Mallik, R.1    Hage, D.S.2
  • 54
    • 13844253750 scopus 로고    scopus 로고
    • Chromatographic investigation of macromolecular affinity interactions
    • Platonova G.A., and Tennikova T.B. Chromatographic investigation of macromolecular affinity interactions. J. Chromatogr. A. 1065 (2005) 75-81
    • (2005) J. Chromatogr. A. , vol.1065 , pp. 75-81
    • Platonova, G.A.1    Tennikova, T.B.2
  • 55
    • 0035975882 scopus 로고    scopus 로고
    • Twenty-five years of immobilized metal ion affinity chromatography: past, present and future
    • Chaga G.S. Twenty-five years of immobilized metal ion affinity chromatography: past, present and future. J. Biochem. Biophys. Methods 49 (2001) 313-334
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 313-334
    • Chaga, G.S.1
  • 56
    • 0038458864 scopus 로고    scopus 로고
    • Nucleic acid separations utilizing immobilized metal affinity chromatography
    • Murphy J.C., et al. Nucleic acid separations utilizing immobilized metal affinity chromatography. Biotechnol. Prog. 19 (2003) 982-986
    • (2003) Biotechnol. Prog. , vol.19 , pp. 982-986
    • Murphy, J.C.1
  • 57
    • 37448998768 scopus 로고    scopus 로고
    • Sequence-specific binding of DNA and RNA to immobilized nickel ions
    • Nastasijevic B., et al. Sequence-specific binding of DNA and RNA to immobilized nickel ions. Biochem. Biophys. Res. Commun. 366 (2008) 420-425
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 420-425
    • Nastasijevic, B.1
  • 58
    • 26644441231 scopus 로고    scopus 로고
    • Separation of genomic DNA from plasmid DNA by selective renaturation with immobilized metal affinity capture
    • Cano T., et al. Separation of genomic DNA from plasmid DNA by selective renaturation with immobilized metal affinity capture. Biotechnol. Prog. 21 (2005) 1472-1477
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1472-1477
    • Cano, T.1
  • 59
    • 33846241366 scopus 로고    scopus 로고
    • Differential interactions of plasmid DNA, RNA and endotoxin with immobilised and free metal ions
    • Tan L., et al. Differential interactions of plasmid DNA, RNA and endotoxin with immobilised and free metal ions. J. Chromatogr. A. 1141 (2007) 226-234
    • (2007) J. Chromatogr. A. , vol.1141 , pp. 226-234
    • Tan, L.1
  • 60
    • 0030979103 scopus 로고    scopus 로고
    • Efficient purification of plasmid DNA for gene transfer using triple-helix affinity chromatography
    • Wils P., et al. Efficient purification of plasmid DNA for gene transfer using triple-helix affinity chromatography. Gene Ther. 4 (1997) 323-330
    • (1997) Gene Ther. , vol.4 , pp. 323-330
    • Wils, P.1
  • 61
    • 0032190243 scopus 로고    scopus 로고
    • Purification of plasmids by triplex affinity interaction
    • Schluep T., and Cooney C.L. Purification of plasmids by triplex affinity interaction. Nucleic Acids Res. 26 (1998) 4524-4528
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4524-4528
    • Schluep, T.1    Cooney, C.L.2
  • 62
    • 0037143805 scopus 로고    scopus 로고
    • Protein-mediated isolation of plasmid DNA by a zinc finger-glutathione S-transferase affinity linker
    • Woodgate J., et al. Protein-mediated isolation of plasmid DNA by a zinc finger-glutathione S-transferase affinity linker. Biotechnol. Bioeng. 79 (2002) 450-456
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 450-456
    • Woodgate, J.1
  • 63
    • 2942746570 scopus 로고    scopus 로고
    • Affinity adsorption of plasmid DNA
    • Ghose S., et al. Affinity adsorption of plasmid DNA. Biotechnol. Prog. 20 (2004) 841-850
    • (2004) Biotechnol. Prog. , vol.20 , pp. 841-850
    • Ghose, S.1
  • 64
    • 20444415980 scopus 로고    scopus 로고
    • Immobilisation of a repressor protein for binding of plasmid DNA
    • Hasche A., and Voss C. Immobilisation of a repressor protein for binding of plasmid DNA. J. Chromatogr. A. 1080 (2005) 76-82
    • (2005) J. Chromatogr. A. , vol.1080 , pp. 76-82
    • Hasche, A.1    Voss, C.2
  • 65
    • 33748433378 scopus 로고    scopus 로고
    • LacO-LacI interaction in affinity adsorption of plasmid DNA
    • Forde G.M., et al. LacO-LacI interaction in affinity adsorption of plasmid DNA. Biotechnol. Bioeng. 95 (2006) 67-75
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 67-75
    • Forde, G.M.1
  • 66
    • 18144406111 scopus 로고    scopus 로고
    • LacI-mediated sequence-specific affinity purification of plasmid DNA for therapeutic applications
    • Darby R.A., and Hine A.V. LacI-mediated sequence-specific affinity purification of plasmid DNA for therapeutic applications. FASEB J. 19 (2005) 801-803
    • (2005) FASEB J. , vol.19 , pp. 801-803
    • Darby, R.A.1    Hine, A.V.2
  • 67
    • 36749084045 scopus 로고    scopus 로고
    • Affinity purification of plasmid DNA directly from crude bacterial cell lysates
    • Darby R.A., et al. Affinity purification of plasmid DNA directly from crude bacterial cell lysates. Biotechnol. Bioeng. 98 (2007) 1103-1108
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 1103-1108
    • Darby, R.A.1
  • 68
    • 0030342252 scopus 로고    scopus 로고
    • Histidine ligand affinity chromatography
    • Vijayalakshmi M.A. Histidine ligand affinity chromatography. Mol. Biotechnol. 6 (1996) 347-357
    • (1996) Mol. Biotechnol. , vol.6 , pp. 347-357
    • Vijayalakshmi, M.A.1
  • 69
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe N.M., et al. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res. 29 (2001) 2860-2874
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1
  • 70
    • 0347755630 scopus 로고    scopus 로고
    • AANT: the Amino Acid-Nucleotide Interaction Database
    • Hoffman M.M., et al. AANT: the Amino Acid-Nucleotide Interaction Database. Nucleic Acids Res. 32 (2004) D174-D181
    • (2004) Nucleic Acids Res. , vol.32
    • Hoffman, M.M.1
  • 71
    • 22144443546 scopus 로고    scopus 로고
    • Separation of supercoiled and open circular plasmid DNA isoforms by chromatography with a histidine-agarose support
    • Sousa F., et al. Separation of supercoiled and open circular plasmid DNA isoforms by chromatography with a histidine-agarose support. Anal. Biochem. 343 (2005) 183-185
    • (2005) Anal. Biochem. , vol.343 , pp. 183-185
    • Sousa, F.1
  • 72
    • 39149129979 scopus 로고    scopus 로고
    • Specific recognition of supercoiled plasmid DNA in arginine affinity chromatography
    • Sousa F., et al. Specific recognition of supercoiled plasmid DNA in arginine affinity chromatography. Anal. Biochem. 374 (2008) 432-434
    • (2008) Anal. Biochem. , vol.374 , pp. 432-434
    • Sousa, F.1
  • 73
    • 33750607427 scopus 로고    scopus 로고
    • Selective purification of supercoiled plasmid DNA from clarified cell lysates with a single histidine-agarose chromatography step
    • Sousa F., et al. Selective purification of supercoiled plasmid DNA from clarified cell lysates with a single histidine-agarose chromatography step. Biotechnol. Appl. Biochem. 45 (2006) 131-140
    • (2006) Biotechnol. Appl. Biochem. , vol.45 , pp. 131-140
    • Sousa, F.1
  • 74
    • 34547966151 scopus 로고    scopus 로고
    • Dynamic binding capacity of plasmid DNA in histidine-agarose chromatography
    • Sousa F., et al. Dynamic binding capacity of plasmid DNA in histidine-agarose chromatography. Biomed. Chromatogr. 21 (2007) 993-998
    • (2007) Biomed. Chromatogr. , vol.21 , pp. 993-998
    • Sousa, F.1
  • 75
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch D., and Anspach F.B. Endotoxin removal from protein solutions. J. Biotechnol. 76 (2000) 97-119
    • (2000) J. Biotechnol. , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2


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