메뉴 건너뛰기




Volumn 110, Issue 9, 2013, Pages 2452-2461

Fast and scalable purification of a therapeutic full-length antibody based on process crystallization

Author keywords

Alternative to chromatography; CHO cell culture harvest; Purification process; Scale up; Stirred process crystallization; Therapeutic monoclonal antibody

Indexed keywords

CHO CELL CULTURES; CRYSTALLIZATION PROCESS; HIGH SALT CONCENTRATION; MONOCLONAL ANTIBODY PURIFICATION; PROTEIN A CHROMATOGRAPHY; PURIFICATION PROCESS; SCALE-UP; THERAPEUTIC MONOCLONAL ANTIBODIES;

EID: 84880790791     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24908     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 84880780391 scopus 로고    scopus 로고
    • A computational tool to predict the protein-protein interaction hot-spot residues from the structure of the unbound protein. Manuscript submitted for publication
    • Agrawal NJ, Helk B, Trout BL. 2012. A computational tool to predict the protein-protein interaction hot-spot residues from the structure of the unbound protein. Manuscript submitted for publication.
    • (2012)
    • Agrawal, N.J.1    Helk, B.2    Trout, B.L.3
  • 2
    • 0002889635 scopus 로고
    • Direct crystallization of lysozyme from egg white and some crystalline salts of lysozyme
    • Alderton G, Fevold HL. 1946. Direct crystallization of lysozyme from egg white and some crystalline salts of lysozyme. J Biol Chem 164:1-5.
    • (1946) J Biol Chem , vol.164 , pp. 1-5
    • Alderton, G.1    Fevold, H.L.2
  • 3
    • 55449104956 scopus 로고    scopus 로고
    • Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
    • Andya JD, Hsu CC, Shire SJ. 2003. Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. AAPS PharmSci 5:21-31.
    • (2003) AAPS PharmSci , vol.5 , pp. 21-31
    • Andya, J.D.1    Hsu, C.C.2    Shire, S.J.3
  • 5
    • 78149348798 scopus 로고    scopus 로고
    • Crystallization of recombinant human growth hormone at elevated pressures: Pressure effects on PEG-induced volume exclusion interactions
    • Crisman RL, Randolph TW. 2010. Crystallization of recombinant human growth hormone at elevated pressures: Pressure effects on PEG-induced volume exclusion interactions. Biotechnol Bioeng 107:663-672.
    • (2010) Biotechnol Bioeng , vol.107 , pp. 663-672
    • Crisman, R.L.1    Randolph, T.W.2
  • 8
    • 0037394598 scopus 로고    scopus 로고
    • Nucleation of protein crystals
    • Garcia-Ruiz JM. 2003. Nucleation of protein crystals. J Struct Biol 142:22-31.
    • (2003) J Struct Biol , vol.142 , pp. 22-31
    • Garcia-Ruiz, J.M.1
  • 9
    • 79955888189 scopus 로고    scopus 로고
    • Urate oxidase purification by salting-in crystallization: Towards an alternative to chromatography
    • Giffard M, Ferte N, Ragot F, El Hajji M, Castro B, Bonnete F. 2011. Urate oxidase purification by salting-in crystallization: Towards an alternative to chromatography. PLoS ONE 6:e19013.
    • (2011) PLoS ONE , vol.6
    • Giffard, M.1    Ferte, N.2    Ragot, F.3    El Hajji, M.4    Castro, B.5    Bonnete, F.6
  • 10
    • 45149110469 scopus 로고    scopus 로고
    • Bioseparation in antibody manufacturing: The good, the bad and the ugly
    • Gottschalk U. 2008. Bioseparation in antibody manufacturing: The good, the bad and the ugly. Biotechnol Prog 24:496-503.
    • (2008) Biotechnol Prog , vol.24 , pp. 496-503
    • Gottschalk, U.1
  • 11
    • 37049207261 scopus 로고
    • Ferritin and apoferritin
    • Granick S, Michaelis L. 1942. Ferritin and apoferritin. Science 95:439-440.
    • (1942) Science , vol.95 , pp. 439-440
    • Granick, S.1    Michaelis, L.2
  • 12
    • 0028846780 scopus 로고
    • Crystallization of intact monoclonal antibodies
    • Harris LJ, Skaletsky E, McPherson A. 1995. Crystallization of intact monoclonal antibodies. Proteins 23:285-289.
    • (1995) Proteins , vol.23 , pp. 285-289
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 13
  • 16
    • 0019860919 scopus 로고
    • Low molecular weight RNAs transcribed in vitro by RNA polymerase III from Alu-type dispersed repeats in Chinese hamster DNA are also found in vivo
    • Haynes SR, Jelinek WR. 1981. Low molecular weight RNAs transcribed in vitro by RNA polymerase III from Alu-type dispersed repeats in Chinese hamster DNA are also found in vivo. Proc Natl Acad Sci USA 78:6130-6134.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6130-6134
    • Haynes, S.R.1    Jelinek, W.R.2
  • 17
    • 36048930506 scopus 로고    scopus 로고
    • Crystallization of lysozyme: From vapor diffusion experiments to batch crystallization in agitated ml-scale vessels
    • Hekmat D, Hebel D, Schmid H, Weuster-Botz D. 2007. Crystallization of lysozyme: From vapor diffusion experiments to batch crystallization in agitated ml-scale vessels. Process Biochem 42:1649-1654.
    • (2007) Process Biochem , vol.42 , pp. 1649-1654
    • Hekmat, D.1    Hebel, D.2    Schmid, H.3    Weuster-Botz, D.4
  • 18
    • 84875021026 scopus 로고
    • On the separation of a pure albumin from egg-white
    • Hopkins FG. 1900. On the separation of a pure albumin from egg-white. J Physiol 25:306-330.
    • (1900) J Physiol , vol.25 , pp. 306-330
    • Hopkins, F.G.1
  • 19
    • 0032549475 scopus 로고    scopus 로고
    • Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths
    • Jacobsen C, Garside J, Hoare M. 1998. Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths. Biotechnol Bioeng 57:666-675.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 666-675
    • Jacobsen, C.1    Garside, J.2    Hoare, M.3
  • 20
    • 33845258911 scopus 로고    scopus 로고
    • Crystallization of IgG1 by mapping its liquid-liquid phase separation curves
    • Jion AI, Goh L-T, Oh SKW. 2006. Crystallization of IgG1 by mapping its liquid-liquid phase separation curves. Biotechnol Bioeng 95:911-918.
    • (2006) Biotechnol Bioeng , vol.95 , pp. 911-918
    • Jion, A.I.1    Goh, L.-T.2    Oh, S.K.W.3
  • 21
    • 0029395001 scopus 로고
    • Protein purification by bulk crystallization: The recovery of ovalbumin
    • Judge RA, Johns MR, White ET. 1995. Protein purification by bulk crystallization: The recovery of ovalbumin. Biotechnol Bioeng 48:316-323.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 316-323
    • Judge, R.A.1    Johns, M.R.2    White, E.T.3
  • 22
    • 0032552493 scopus 로고    scopus 로고
    • The effect of protein impurities on lysozyme crystal growth
    • Judge RA, Forsythe EL, Pusey ML. 1998. The effect of protein impurities on lysozyme crystal growth. Biotechnol Bioeng 59:776-785.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 776-785
    • Judge, R.A.1    Forsythe, E.L.2    Pusey, M.L.3
  • 23
    • 0023601122 scopus 로고
    • Automated production scale affinity purification of monoclonal antibodies
    • Kenney AC, Chase HA. 1987. Automated production scale affinity purification of monoclonal antibodies. J Chem Technol Biotechnol 39:173-182.
    • (1987) J Chem Technol Biotechnol , vol.39 , pp. 173-182
    • Kenney, A.C.1    Chase, H.A.2
  • 24
    • 0035847162 scopus 로고    scopus 로고
    • Membrane ion-exchange chromatography for process-scale antibody purification
    • Knudsen HL, Fahrner RL, Xu Y, Norling LA, Blank GS. 2001. Membrane ion-exchange chromatography for process-scale antibody purification. J Chromatogr A 907:145-154.
    • (2001) J Chromatogr A , vol.907 , pp. 145-154
    • Knudsen, H.L.1    Fahrner, R.L.2    Xu, Y.3    Norling, L.A.4    Blank, G.S.5
  • 25
    • 74849134337 scopus 로고    scopus 로고
    • Development of a polishing step using a hydrophobic interaction membrane adsorber with a PER.C6-derived recombinant antibody
    • Kuczewski M, Fraud N, Faber R, Zarbis-Papastoitsis G. 2010. Development of a polishing step using a hydrophobic interaction membrane adsorber with a PER.C6-derived recombinant antibody. Biotechnol Bioeng 105:296-305.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 296-305
    • Kuczewski, M.1    Fraud, N.2    Faber, R.3    Zarbis-Papastoitsis, G.4
  • 26
    • 0026005265 scopus 로고
    • Characterization of crystals of an intact monoclonal antibody for canine lymphoma
    • Larson S, Day J, Greenwood A, Skaletsky E, McPherson A. 1991. Characterization of crystals of an intact monoclonal antibody for canine lymphoma. J Mol Biol 222:17-19.
    • (1991) J Mol Biol , vol.222 , pp. 17-19
    • Larson, S.1    Day, J.2    Greenwood, A.3    Skaletsky, E.4    McPherson, A.5
  • 27
    • 82255192512 scopus 로고    scopus 로고
    • Developability index: A rapid in silico tool for the screening of antibody aggregation propensity
    • Lauer TM, Agrawal NJ, Chennamsetty N, Egodage K, Helk B, Trout BL. 2012. Developability index: A rapid in silico tool for the screening of antibody aggregation propensity. J Pharm Sci 101:102-115.
    • (2012) J Pharm Sci , vol.101 , pp. 102-115
    • Lauer, T.M.1    Agrawal, N.J.2    Chennamsetty, N.3    Egodage, K.4    Helk, B.5    Trout, B.L.6
  • 29
    • 77958589701 scopus 로고    scopus 로고
    • Recovery and purification process development for monoclonal antibody production
    • Liu HF, Ma J, Winter C, Bayer R. 2010. Recovery and purification process development for monoclonal antibody production. MAbs 2:480-499.
    • (2010) MAbs , vol.2 , pp. 480-499
    • Liu, H.F.1    Ma, J.2    Winter, C.3    Bayer, R.4
  • 32
    • 0035907697 scopus 로고    scopus 로고
    • Protein crystals as novel catalytic materials
    • Margolin AL, Navia MA. 2001. Protein crystals as novel catalytic materials. Angew Chem Int Ed Engl 40:2204-2222.
    • (2001) Angew Chem Int Ed Engl , vol.40 , pp. 2204-2222
    • Margolin, A.L.1    Navia, M.A.2
  • 33
    • 0031950561 scopus 로고    scopus 로고
    • Protein-protein interactions as a means of purification
    • Przybycien TM. 1998. Protein-protein interactions as a means of purification. Curr Opin Biotechnol 9:164-170.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 164-170
    • Przybycien, T.M.1
  • 34
    • 84866264970 scopus 로고    scopus 로고
    • Full automation and validation of a flexible ELISA platform for host cell protein and protein A impurity detection in biopharmaceuticals
    • Rey G, Wendeler MW. 2012. Full automation and validation of a flexible ELISA platform for host cell protein and protein A impurity detection in biopharmaceuticals. J Pharm Biomed Anal 70:580-586.
    • (2012) J Pharm Biomed Anal , vol.70 , pp. 580-586
    • Rey, G.1    Wendeler, M.W.2
  • 39
    • 0001470914 scopus 로고
    • The isolation and crystallization of the enzyme urease: Preliminary paper
    • Sumner JB. 1926. The isolation and crystallization of the enzyme urease: Preliminary paper. J Biol Chem 69:435-441.
    • (1926) J Biol Chem , vol.69 , pp. 435-441
    • Sumner, J.B.1
  • 41
    • 79961027385 scopus 로고    scopus 로고
    • Crystallization and liquid-liquid phase separation of monoclonal antibodies and Fc-fusion proteins: Screening results
    • Trilisky E, Gillespie R, Osslund TD, Vunnum S. 2011. Crystallization and liquid-liquid phase separation of monoclonal antibodies and Fc-fusion proteins: Screening results. Biotechnol Prog 27:1054-1067.
    • (2011) Biotechnol Prog , vol.27 , pp. 1054-1067
    • Trilisky, E.1    Gillespie, R.2    Osslund, T.D.3    Vunnum, S.4
  • 42
    • 41849116376 scopus 로고    scopus 로고
    • Optimisation of isolation and purification of the jack bean enzyme urease by extraction and subsequent crystallization
    • Weber M, Jones MJ, Ulrich J. 2008. Optimisation of isolation and purification of the jack bean enzyme urease by extraction and subsequent crystallization. Food Bioprod Process 86:43-52.
    • (2008) Food Bioprod Process , vol.86 , pp. 43-52
    • Weber, M.1    Jones, M.J.2    Ulrich, J.3
  • 43
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm FM. 2004. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol 22:1393-1398.
    • (2004) Nat Biotechnol , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 45
    • 80053090101 scopus 로고    scopus 로고
    • Towards protein crystallization as a process step in downstream processing of therapeutic antibodies: Screening and optimization at microbatch scale
    • Zang Y, Kammerer B, Eisenkolb M, Lohr K, Kiefer H. 2011. Towards protein crystallization as a process step in downstream processing of therapeutic antibodies: Screening and optimization at microbatch scale. PLoS ONE 6:e25282.
    • (2011) PLoS ONE , vol.6
    • Zang, Y.1    Kammerer, B.2    Eisenkolb, M.3    Lohr, K.4    Kiefer, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.