메뉴 건너뛰기




Volumn , Issue , 2006, Pages 541-564

A membrane chromatography application: A rapid, high capacity gene therapy vector purification tool

Author keywords

[No Author keywords available]

Indexed keywords


EID: 62249087446     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (5)

References (72)
  • 1
    • 0038745599 scopus 로고    scopus 로고
    • Progress and problems with the use of viral vectors for gene therapy
    • Thomas CE, Ehrhardt A, and Kay MA. Progress and problems with the use of viral vectors for gene therapy. Nat. Rev. Genet. 2003, 4:346-358.
    • (2003) Nat. Rev. Genet , vol.4 , pp. 346-358
    • Thomas, C.E.1    Ehrhardt, A.2    Kay, M.A.3
  • 3
    • 85123450791 scopus 로고    scopus 로고
    • (accessed January 5)
    • http://www.wiley.co.uk/genetherapy/clinical/ (accessed January 5, 2005).
    • (2005)
  • 4
    • 85123419450 scopus 로고    scopus 로고
    • Adenoviridae: The viruses and their replication
    • Kinpe DM and Howley PM, Eds. Lipincott Williams and Wilkins, Philadelphia
    • Shenk TE. Adenoviridae: The viruses and their replication. In: Virology. Kinpe DM and Howley PM, Eds. Lipincott Williams and Wilkins, Philadelphia, pp. 2201, 2265-2300.
    • Virology
    • Shenk, T.E.1
  • 7
    • 2642642141 scopus 로고    scopus 로고
    • Production of high-titer recombinant adeno-associated virus vectors in the absence of helper adenovirus
    • Xiao X, Li J, and Samulski RJ. Production of high-titer recombinant adeno-associated virus vectors in the absence of helper adenovirus. J. Virol. 1998, 72:2224-2232.
    • (1998) J. Virol , vol.72 , pp. 2224-2232
    • Xiao, X.1    Li, J.2    Samulski, R.J.3
  • 8
    • 0032506752 scopus 로고    scopus 로고
    • Novel tools for production and purification of recombinant adeno-associated virus vectors
    • Grimm D, Kern A, Rittner K, and Kleinschmidt JA. Novel tools for production and purification of recombinant adeno-associated virus vectors. Hum. Gene Ther. 1998, 9:2745-2760.
    • (1998) Hum. Gene Ther , vol.9 , pp. 2745-2760
    • Grimm, D.1    Kern, A.2    Rittner, K.3    Kleinschmidt, J.A.4
  • 9
    • 0037333336 scopus 로고    scopus 로고
    • Latest development in viral vectors for gene therapy
    • Lundstrom K. Latest development in viral vectors for gene therapy. Trends Biotechnol. 2003, 21:117-122.
    • (2003) Trends Biotechnol , vol.21 , pp. 117-122
    • Lundstrom, K.1
  • 10
    • 4644346385 scopus 로고    scopus 로고
    • Improving rAAV production and purification: Towards the definition of a scaleable process
    • Blouin V, Brument N, Toublanc E, Raimbaud I, Moullier P, and Salvetti A. Improving rAAV production and purification: towards the definition of a scaleable process. J. Gene Med. 2004, 6:S223-S228.
    • (2004) J. Gene Med , vol.6 , pp. S223-S228
    • Blouin, V.1    Brument, N.2    Toublanc, E.3    Raimbaud, I.4    Moullier, P.5    Salvetti, A.6
  • 11
    • 0032845129 scopus 로고    scopus 로고
    • Process and product development in the manufacturing of molecular therapeutics
    • Atkinson M and Christensen J. Process and product development in the manufacturing of molecular therapeutics. Curr. Opin. Mol. Ther. 1999, 1:422-429.
    • (1999) Curr. Opin. Mol. Ther , vol.1 , pp. 422-429
    • Atkinson, M.1    Christensen, J.2
  • 13
    • 0036371516 scopus 로고    scopus 로고
    • Oncoretroviral and lentiviral vector-mediated gene therapy
    • New York: Academic Press
    • Vanden Driessche T, Naldini L, Collen D, and Chuah MKL. Oncoretroviral and lentiviral vector-mediated gene therapy. In: Methods in Enzymology, Vol. 346, New York: Academic Press, 2002, pp. 573-589.
    • (2002) Methods in Enzymology , vol.346 , pp. 573-589
    • Vanden Driessche, T.1    Naldini, L.2    Collen, D.3    Chuah, M.K.L.4
  • 14
    • 0036235391 scopus 로고    scopus 로고
    • Retroviral vectors for human gene delivery
    • McTaggart S and Al-Rubeai M. Retroviral vectors for human gene delivery. Biotechnol. Adv. 2002; 20:1-31.
    • (2002) Biotechnol. Adv , vol.20 , pp. 1-31
    • McTaggart, S.1    Al-Rubeai, M.2
  • 16
    • 3042786314 scopus 로고    scopus 로고
    • DNA Vaccines-back in the saddle again
    • Powell K. DNA Vaccines-back in the saddle again. Nat. Biotechnol. 2004, 22:799-801.
    • (2004) Nat. Biotechnol , vol.22 , pp. 799-801
    • Powell, K.1
  • 18
    • 0035810734 scopus 로고    scopus 로고
    • Improved highperformance liquid chromatographic method in the analysis of adenovirus particles
    • Klyushnichenko V, Bernier A, Kamen A, and Harmsen E. Improved highperformance liquid chromatographic method in the analysis of adenovirus particles. J. Chromatogr. B 2001, 755:27-36.
    • (2001) J. Chromatogr. B , vol.755 , pp. 27-36
    • Klyushnichenko, V.1    Bernier, A.2    Kamen, A.3    Harmsen, E.4
  • 19
    • 0028242168 scopus 로고
    • Purification of viruses and macromolecular assemblies for the structural investigatios using a novel ion exchange method
    • Wanlin L, Tuma R, Thomas GJ, and Bamford DH. Purification of viruses and macromolecular assemblies for the structural investigatios using a novel ion exchange method. Virology 1994, 201:1-7.
    • (1994) Virology , vol.201 , pp. 1-7
    • Wanlin, L.1    Tuma, R.2    Thomas, G.J.3    Bamford, D.H.4
  • 20
    • 0021062903 scopus 로고
    • Purification of barley yellow dwarf virus by gel filtration on Sephacryl S-1000 Superfine
    • Hewish D and Shukla D. Purification of barley yellow dwarf virus by gel filtration on Sephacryl S-1000 Superfine. J. Virol. Meth. 1983, 7:223-228.
    • (1983) J. Virol. Meth , vol.7 , pp. 223-228
    • Hewish, D.1    Shukla, D.2
  • 21
    • 0020333974 scopus 로고
    • Purification of bovine papilloma virus by gel filtration on Sephacryl S-1000 Superfine
    • Hjorth R and Moreno-Lopez J. Purification of bovine papilloma virus by gel filtration on Sephacryl S-1000 Superfine. J. Virol. Meth. 1982, 5:151-158.
    • (1982) J. Virol. Meth , vol.5 , pp. 151-158
    • Hjorth, R.1    Moreno-Lopez, J.2
  • 22
    • 85123440486 scopus 로고    scopus 로고
    • Development of a novel adenovirus purification process utilizing selective precipitation of cellular DNA
    • Goerke AR, To BCS, Lee AL, Sagar SL, and Konz JO. Development of a novel adenovirus purification process utilizing selective precipitation of cellular DNA. Biotechnol. Bioeng. 2005, 83:45-52.
    • (2005) Biotechnol. Bioeng , vol.83 , pp. 45-52
    • Goerke, A.R.1    To, B.C.S.2    Lee, A.L.3    Sagar, S.L.4    Konz, J.O.5
  • 24
    • 3042704538 scopus 로고    scopus 로고
    • Development and optimization of an adenovirus production process
    • Kamen A and Henry O. Development and optimization of an adenovirus production process. J. Gene Med. 2004, 6:S184-S192.
    • (2004) J. Gene Med , vol.6 , pp. S184-S192
    • Kamen, A.1    Henry, O.2
  • 25
    • 0141436697 scopus 로고    scopus 로고
    • Adenovirus type 5 (Ad5) chromatographic purification process at 20L scale
    • Arcand N, Bernier A, and Transfiguracion J. Adenovirus type 5 (Ad5) chromatographic purification process at 20L scale. Bioprocess. J. 2003, 2:72-75.
    • (2003) Bioprocess. J , vol.2 , pp. 72-75
    • Arcand, N.1    Bernier, A.2    Transfiguracion, J.3
  • 26
    • 5644244895 scopus 로고    scopus 로고
    • Large-scale production, purification and crystallization of wild-type adeno-associated Virus-2
    • Xie Q, Hare J, Turnigan J, and Chapman MS. Large-scale production, purification and crystallization of wild-type adeno-associated Virus-2. J. Virol. Meth. 2004, 122:17-27.
    • (2004) J. Virol. Meth , vol.122 , pp. 17-27
    • Xie, Q.1    Hare, J.2    Turnigan, J.3    Chapman, M.S.4
  • 27
    • 0034766041 scopus 로고    scopus 로고
    • A single-step affinity column for purification of serotype-5 based adeno-associated viral vectors
    • Auricchio A, O'Connor E, Hildinger M, and Wilson JM. A single-step affinity column for purification of serotype-5 based adeno-associated viral vectors. Mol. Ther. 2001, 4:372-374.
    • (2001) Mol. Ther , vol.4 , pp. 372-374
    • Auricchio, A.1    O'Connor, E.2    Hildinger, M.3    Wilson, J.M.4
  • 28
    • 0033541640 scopus 로고    scopus 로고
    • Highly purified recombinant adeno-associated virus vectors are biologically active and free of detectable helper and wild-type viruses
    • Clark RK, Liu X, McGrath JP, and Johnson PR. Highly purified recombinant adeno-associated virus vectors are biologically active and free of detectable helper and wild-type viruses. Hum. Gene Ther. 1999, 10:1031-1039.
    • (1999) Hum. Gene Ther , vol.10 , pp. 1031-1039
    • Clark, R.K.1    Liu, X.2    McGrath, J.P.3    Johnson, P.R.4
  • 30
    • 0036811528 scopus 로고    scopus 로고
    • Production of clinical-grade recombinant adeno-associated virus vectors
    • Synder RO and Flotte TR. Production of clinical-grade recombinant adeno-associated virus vectors. Curr. Opin. Biotechnol. 2002, 13:418-423.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 418-423
    • Synder, R.O.1    Flotte, T.R.2
  • 32
    • 0036019204 scopus 로고    scopus 로고
    • Scalable purification of adeno-associated virus type 2, 4, or 5 using ion-exchange chromatography
    • Kaludov N, Handelman B, and Chiorini J. Scalable purification of adeno-associated virus type 2, 4, or 5 using ion-exchange chromatography. Hum. Gene Ther. 2002, 13:1235-1243.
    • (2002) Hum. Gene Ther , vol.13 , pp. 1235-1243
    • Kaludov, N.1    Handelman, B.2    Chiorini, J.3
  • 34
    • 0242643501 scopus 로고    scopus 로고
    • Serum-free production and column purification of adeno-associated virus type 5
    • Smith RH, Ding C, and Kotin RM. Serum-free production and column purification of adeno-associated virus type 5. J. Virol. Meth. 2003,114:115-124.
    • (2003) J. Virol. Meth , vol.114 , pp. 115-124
    • Smith, R.H.1    Ding, C.2    Kotin, R.M.3
  • 35
    • 0242382679 scopus 로고    scopus 로고
    • Optimized lentiviral vector production and purification procedure prevents immune response after transduction of mouse brain
    • Baekelandt T, Eggermont K, Michiels M, Nuttin B, and Debyser Z. Optimized lentiviral vector production and purification procedure prevents immune response after transduction of mouse brain. Gene Ther. 2003, 10:1933-1940.
    • (2003) Gene Ther , vol.10 , pp. 1933-1940
    • Baekelandt, T.1    Eggermont, K.2    Michiels, M.3    Nuttin, B.4    Debyser, Z.5
  • 36
    • 0038666499 scopus 로고    scopus 로고
    • Lentivirus vector purification using anion exchange HPLC leads to improved gene transfer
    • Yamada K, MacCarty DM, Madden VJ, and Walsh CE. Lentivirus vector purification using anion exchange HPLC leads to improved gene transfer. Biotechniques 2003, 34:1074-1078.
    • (2003) Biotechniques , vol.34 , pp. 1074-1078
    • Yamada, K.1    MacCarty, D.M.2    Madden, V.J.3    Walsh, C.E.4
  • 37
    • 0036957811 scopus 로고    scopus 로고
    • Efficient gene transfer into the CNS by lentiviral vectors purified by anion exchange chromatography
    • Scherr M, Battmer K, Eder M, Schule S, Hohenberg H, Gasner A, Grez M, and Blomer U. Efficient gene transfer into the CNS by lentiviral vectors purified by anion exchange chromatography. Gene Ther. 2002, 9:1708-1714.
    • (2002) Gene Ther , vol.9 , pp. 1708-1714
    • Scherr, M.1    Battmer, K.2    Eder, M.3    Schule, S.4    Hohenberg, H.5    Gasner, A.6    Grez, M.7    Blomer, U.8
  • 38
    • 1242318628 scopus 로고    scopus 로고
    • Lentiviral vectors pseudotyped with baculovirus gp64 efficiently transduce mouse cells in vivo and show tropism restriction against hematopoietic cell types in vitro
    • Schauber, CA, Tuerk MJ, Pacheco CD, Escarpe PA, and Veres, G. Lentiviral vectors pseudotyped with baculovirus gp64 efficiently transduce mouse cells in vivo and show tropism restriction against hematopoietic cell types in vitro. Gene Ther. 2004, 11:266-275.
    • (2004) Gene Ther , vol.11 , pp. 266-275
    • Schauber, C.A.1    Tuerk, M.J.2    Pacheco, C.D.3    Escarpe, P.A.4    Veres, G.5
  • 41
    • 0000590339 scopus 로고    scopus 로고
    • Issues of large-scale plasmid DNA manufacturing
    • Rohm HJ and Reed G, Eds. New York: Wiley-VCH
    • Scheelf M. Issues of large-scale plasmid DNA manufacturing. In: Rohm HJ and Reed G, Eds. Recombinant Proteins, Monoclonal Antibodies and Therapeutic Genes. New York: Wiley-VCH, 1999, pp. 443-469.
    • (1999) Recombinant Proteins, Monoclonal Antibodies and Therapeutic Genes , pp. 443-469
    • Scheelf, M.1
  • 42
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim HC and Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979, 7:1513-1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 43
    • 0038512445 scopus 로고    scopus 로고
    • Large-scale capture and partial purification of plasmid DNA using anion exchange membrane capsules
    • Zhang S, Krivosheyeva A, and Nochumson S. Large-scale capture and partial purification of plasmid DNA using anion exchange membrane capsules. Biotechnol. Appl. Biochem. 2003, 37:245-249.
    • (2003) Biotechnol. Appl. Biochem , vol.37 , pp. 245-249
    • Zhang, S.1    Krivosheyeva, A.2    Nochumson, S.3
  • 44
    • 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 2004, 804:327-335.
    • (2004) J. Chromatogr. B , vol.804 , pp. 327-335
    • Eon-Duval, A.1    Burke, G.2
  • 45
    • 0032496250 scopus 로고    scopus 로고
    • Preparative purification of supercoiled plasmid DNA using anion exchange chromatography
    • Prazeres DMF, Schluep T, and Cooney C. Preparative purification of supercoiled plasmid DNA using anion exchange chromatography. J. Chromatogr. A 1998, 806:31-45.
    • (1998) J. Chromatogr. A , vol.806 , pp. 31-45
    • Prazeres, D.M.F.1    Schluep, T.2    Cooney, C.3
  • 46
    • 0033990180 scopus 로고    scopus 로고
    • Removal of contaminant nucleic acids by nitrocellulose filtration during pharmaceutical-grade plasmid DNA processing
    • Levy MS, Collins IJ, Tsai JT, Shamlou PA, Ward JM, and Dunnill P. Removal of contaminant nucleic acids by nitrocellulose filtration during pharmaceutical-grade plasmid DNA processing. J. Biotechnol. 2000, 76:197-205.
    • (2000) J. Biotechnol , vol.76 , pp. 197-205
    • Levy, M.S.1    Collins, I.J.2    Tsai, J.T.3    Shamlou, P.A.4    Ward, J.M.5    Dunnill, P.6
  • 47
    • 0020787858 scopus 로고
    • Large-scale isolation of plasmid DNA and purification of l phage DNA using hydroxyapatite chromatography
    • Johnson TR and Han J. Large-scale isolation of plasmid DNA and purification of l phage DNA using hydroxyapatite chromatography. Anal. Biochem. 1983, 132:20-25.
    • (1983) Anal. Biochem , vol.132 , pp. 20-25
    • Johnson, T.R.1    Han, J.2
  • 48
    • 0034434790 scopus 로고    scopus 로고
    • Comparison of different types of ceramic hydroxyapatite for the chromatographic separation of plasmid DNA and a recombinant anti-rhesus D antibody
    • Giovannini R and Freitag R. Comparison of different types of ceramic hydroxyapatite for the chromatographic separation of plasmid DNA and a recombinant anti-rhesus D antibody. Bioseparation 2001, 9:359-368.
    • (2001) Bioseparation , vol.9 , pp. 359-368
    • Giovannini, R.1    Freitag, R.2
  • 49
    • 6344285524 scopus 로고    scopus 로고
    • Case study: Capacity challenges in chromatography-based purification of plasmid DNA
    • Rathore AS and Velayudhan A, Eds. New York: Marcel Dekker
    • Sagar SL, Watson MP, and Lee AL. Case study: capacity challenges in chromatography-based purification of plasmid DNA. In: Rathore AS and Velayudhan A, Eds. Scale-Up and Optimization in Preparative Chromato-graphy. New York: Marcel Dekker, 2003, pp. 251-272.
    • (2003) Scale-Up and Optimization in Preparative Chromato-graphy , pp. 251-272
    • Sagar, S.L.1    Watson, M.P.2    Lee, A.L.3
  • 50
    • 0028978028 scopus 로고
    • Cancer gene therapy using plasmid DNA: Purification of DNA for human clinical trials
    • Horn N, Meek JA, Budahazi G, and Marquet M. Cancer gene therapy using plasmid DNA: purification of DNA for human clinical trials. Hum. Gene Ther. 1995, 6:565-573.
    • (1995) Hum. Gene Ther , vol.6 , pp. 565-573
    • Horn, N.1    Meek, J.A.2    Budahazi, G.3    Marquet, M.4
  • 52
    • 0037402921 scopus 로고    scopus 로고
    • Removal of RNA impurities by tangential flow filtration in an RNase-free plasmid DNA purification process
    • Eon-Duval A, MacDuff RH, Fisher CA, Harris MJ, and Brook C. Removal of RNA impurities by tangential flow filtration in an RNase-free plasmid DNA purification process. Anal. Biochem. 2003, 316:66-73.
    • (2003) Anal. Biochem , vol.316 , pp. 66-73
    • Eon-Duval, A.1    MacDuff, R.H.2    Fisher, C.A.3    Harris, M.J.4    Brook, C.5
  • 55
    • 0028860046 scopus 로고
    • Membrane chromatography - an integrative concept in the downstream processing of proteins
    • Thommes J and Kula MR. Membrane chromatography - an integrative concept in the downstream processing of proteins. Biotechnol Prog 1995, 11:357-367.
    • (1995) Biotechnol Prog , vol.11 , pp. 357-367
    • Thommes, J.1    Kula, M.R.2
  • 56
    • 0032006744 scopus 로고    scopus 로고
    • Purification of proteins by membrane chromatography
    • Charcosset C. Purification of proteins by membrane chromatography. J. Chem. Technol. Biotechnol. 1998, 71, 95-110.
    • (1998) J. Chem. Technol. Biotechnol , vol.71 , pp. 95-110
    • Charcosset, C.1
  • 57
    • 0037023369 scopus 로고    scopus 로고
    • Protein separation using membrane chromatography: Opportunities and challenges
    • Ghose R. Protein separation using membrane chromatography: opportunities and challenges. J. Chromatogr. A 2002, 952:13-27.
    • (2002) J. Chromatogr. A , vol.952 , pp. 13-27
    • Ghose, R.1
  • 58
    • 0034669857 scopus 로고    scopus 로고
    • Affinity membranes a 10-year review
    • Klein E. Affinity membranes a 10-year review. J. Membr. Sci. 2000, 179:1-27.
    • (2000) J. Membr. Sci , vol.179 , pp. 1-27
    • Klein, E.1
  • 59
    • 0032998971 scopus 로고    scopus 로고
    • Direct visualization of plasmid DNA in individual chromatography adsorbent particles by confocal scanning laser microscopy
    • Ljunglof A, Bergvall P, Bhikhabhai R, and Hjorth R. Direct visualization of plasmid DNA in individual chromatography adsorbent particles by confocal scanning laser microscopy. J. Chromatogr. A 1999, 844: 129-135.
    • (1999) J. Chromatogr. A , vol.844 , pp. 129-135
    • Ljunglof, A.1    Bergvall, P.2    Bhikhabhai, R.3    Hjorth, R.4
  • 61
    • 0029070303 scopus 로고
    • Estimating plate heights in stacked-membrane chromatography by flow reversal
    • Roper DK and Lightfoot EN. Estimating plate heights in stacked-membrane chromatography by flow reversal. J. Chromatogr. A 1995, 702:69-80.
    • (1995) J. Chromatogr. A , vol.702 , pp. 69-80
    • Roper, D.K.1    Lightfoot, E.N.2
  • 63
    • 0035450914 scopus 로고    scopus 로고
    • Plasmid purification using membrane-based anion-exchange chromatography
    • Grunwald AG and Shields MS. Plasmid purification using membrane-based anion-exchange chromatography. Anal. Biochem. 2001, 296:138-141.
    • (2001) Anal. Biochem , vol.296 , pp. 138-141
    • Grunwald, A.G.1    Shields, M.S.2
  • 64
    • 4344612043 scopus 로고    scopus 로고
    • Characterization of methacrylate monoliths for purification of DNA molecules
    • Bencina M, Podgornik A, and Strancar A. Characterization of methacrylate monoliths for purification of DNA molecules. J. Sep. Sci. 2004, 27:801-810.
    • (2004) J. Sep. Sci , vol.27 , pp. 801-810
    • Bencina, M.1    Podgornik, A.2    Strancar, A.3
  • 65
    • 0036063663 scopus 로고    scopus 로고
    • Evaluation of accuracy and precision of aden-ovirus absorptivity at 260 nm under conditions of complete DNA disruption
    • Sweeney JA and Hennessey JP. Evaluation of accuracy and precision of aden-ovirus absorptivity at 260 nm under conditions of complete DNA disruption. J. Virol. 2002, 295:284-288.
    • (2002) J. Virol , vol.295 , pp. 284-288
    • Sweeney, J.A.1    Hennessey, J.P.2
  • 66
    • 85123417273 scopus 로고    scopus 로고
    • 2nd Annual Viral Vectors and Vaccines Conference, the Williamsburg Biopro-cessing Foundation, WilBio-Europe, Amsterdam, May 25-27
    • Weggeman M. Development of an Ad35-based Malaria Candidate Vaccine. 2nd Annual Viral Vectors and Vaccines Conference, the Williamsburg Biopro-cessing Foundation, WilBio-Europe, Amsterdam, May 25-27, 2005.
    • (2005) Development of an Ad35-based Malaria Candidate Vaccine
    • Weggeman, M.1
  • 67
    • 16344374932 scopus 로고    scopus 로고
    • Development of a purification process for adenovirus: Controlling virus aggregation to improve the clearance of host cell DNA
    • Konz JO, Lee AL, Lewis JA, and Sagar SL. Development of a purification process for adenovirus: controlling virus aggregation to improve the clearance of host cell DNA. Biotechnol. Prog. 2005, 21:466-472.
    • (2005) Biotechnol. Prog , vol.21 , pp. 466-472
    • Konz, J.O.1    Lee, A.L.2    Lewis, J.A.3    Sagar, S.L.4
  • 68
    • 4644321610 scopus 로고    scopus 로고
    • Purification of recombinant adeno-associated virus type 8 vectors by ion-exchange chromatography generates clinical grade vector stock
    • Davidoff AM, Ng CYC, Sleep S, Gray J, Azam S, Zhao Y, Mcintosh JH, Karimipoor M, and Nathwani AC. Purification of recombinant adeno-associated virus type 8 vectors by ion-exchange chromatography generates clinical grade vector stock. J. Virol. Meth. 2005, 121:209-215.
    • (2005) J. Virol. Meth , vol.121 , pp. 209-215
    • Davidoff, A.M.1    Ng, C.Y.C.2    Sleep, S.3    Gray, J.4    Azam, S.5    Zhao, Y.6    Mcintosh, J.H.7    Karimipoor, M.8    Nathwani, A.C.9
  • 70
  • 72
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch D and Anspach FB. Endotoxin removal from protein solutions. J. Biotechnol. 2000, 76:97-119.
    • (2000) J. Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.