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Volumn 27, Issue 4, 2011, Pages 1054-1067

Crystallization and liquid-liquid phase separation of monoclonal antibodies and fc-fusion proteins: Screening results

Author keywords

Crystal; Evaporative screening; Fc fusion; IgG; Liquid liquid separation; Phase behavior; Product precipitation; Self buffering formulation

Indexed keywords

EVAPORATIVE SCREENING; FC-FUSION; IGG; LIQUID-LIQUID SEPARATION; PRODUCT PRECIPITATION; SELF-BUFFERING;

EID: 79961027385     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.621     Document Type: Article
Times cited : (45)

References (49)
  • 2
    • 79961030511 scopus 로고
    • Subtilisin crystallization process. US Patent 5041377
    • Becker T, Lawlis VBJr. Subtilisin crystallization process. US Patent 5041377, 1991.
    • (1991)
    • Becker, T.1    Lawlis Jr, V.B.2
  • 3
    • 0347719515 scopus 로고    scopus 로고
    • Protein crystallization: from HTS to kilogram-scale
    • Klyushnichenko VE. Protein crystallization: from HTS to kilogram-scale. Curr Opin Drug Discov Devel. 2003; 6: 848-854.
    • (2003) Curr Opin Drug Discov Devel. , vol.6 , pp. 848-854
    • Klyushnichenko, V.E.1
  • 4
    • 79961023894 scopus 로고
    • Process for the crystallization of the ammonium and alkali metal salts in insulin. US Patent 3719655
    • Jackson RL. Process for the crystallization of the ammonium and alkali metal salts in insulin. US Patent 3719655, 1973.
    • (1973)
    • Jackson, R.L.1
  • 5
    • 79961030028 scopus 로고    scopus 로고
    • Method for the crystallization of human serum albumin. US Patent 7087719
    • Visuri K, Uotila S, Fulton SP, Couto DE. Method for the crystallization of human serum albumin. US Patent 7087719, 2006.
    • (2006)
    • Visuri, K.1    Uotila, S.2    Fulton, S.P.3    Couto, D.E.4
  • 6
    • 10644257654 scopus 로고    scopus 로고
    • Implementation of a crystallization step into the purification process of a recombinant protein
    • Peters J, Minuth T, Schroder W. Implementation of a crystallization step into the purification process of a recombinant protein. Protein Expr Purif. 2005; 39: 43-53.
    • (2005) Protein Expr Purif. , vol.39 , pp. 43-53
    • Peters, J.1    Minuth, T.2    Schroder, W.3
  • 9
    • 79961025035 scopus 로고    scopus 로고
    • Crystallization of anti-cd20 antibodies. application PCT/US2008/087008
    • Wilkins JA, Oshodi SA, Lobo B, Breece TN. Crystallization of anti-cd20 antibodies. application PCT/US2008/087008, 2009.
    • (2009)
    • Wilkins, J.A.1    Oshodi, S.A.2    Lobo, B.3    Breece, T.N.4
  • 10
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology: the bioprocessing industry at a crossroads
    • Kelley B. Industrialization of mAb production technology: the bioprocessing industry at a crossroads. mAbs. 2009; 1: 1-10.
    • (2009) mAbs. , vol.1 , pp. 1-10
    • Kelley, B.1
  • 12
    • 4744342353 scopus 로고    scopus 로고
    • Alternative bioseparation operations: life beyond packed-bed chromatography
    • Przybycien TM, Pujar NS, Steele LM. Alternative bioseparation operations: life beyond packed-bed chromatography. Curr Opin Biotechnol. 2004; 15: 469-478.
    • (2004) Curr Opin Biotechnol. , vol.15 , pp. 469-478
    • Przybycien, T.M.1    Pujar, N.S.2    Steele, L.M.3
  • 13
    • 33847102715 scopus 로고    scopus 로고
    • Alternatives to chromatographic separations
    • Thommes J, Etzel M. Alternatives to chromatographic separations. Biotechnol Prog. 2007; 23: 42-45.
    • (2007) Biotechnol Prog. , vol.23 , pp. 42-45
    • Thommes, J.1    Etzel, M.2
  • 14
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J. Challenges in the development of high protein concentration formulations. J Pharm Sci. 2004; 93: 1390-1402.
    • (2004) J Pharm Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 17
    • 5044250423 scopus 로고    scopus 로고
    • Protein isoelectric point as a predictor for increased crystallization screening efficiency
    • Kantardjieff KA, Rupp B. Protein isoelectric point as a predictor for increased crystallization screening efficiency. Bioinformatics. 2004; 20: 2162-2168.
    • (2004) Bioinformatics. , vol.20 , pp. 2162-2168
    • Kantardjieff, K.A.1    Rupp, B.2
  • 18
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George A, Wilson WW. Predicting protein crystallization from a dilute solution property. Acta Cryst. 1994; D50: 361-365.
    • (1994) Acta Cryst. , vol.D50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 19
    • 0033513738 scopus 로고    scopus 로고
    • Why is the osmotic second virial coefficient related to protein crystallization?
    • Neal BL, Asthagiri D, Velev OD, Lenhoff AM, Kaler EW. Why is the osmotic second virial coefficient related to protein crystallization? J Cryst Growth. 1999; 196: 377-387.
    • (1999) J Cryst Growth. , vol.196 , pp. 377-387
    • Neal, B.L.1    Asthagiri, D.2    Velev, O.D.3    Lenhoff, A.M.4    Kaler, E.W.5
  • 20
    • 34247207152 scopus 로고    scopus 로고
    • Crystallization conditions of membrane protein CLC-ec1: an example outside the crystallization slot
    • Blouwolff J, Fraden S. Crystallization conditions of membrane protein CLC-ec1: an example outside the crystallization slot. J Cryst Growth. 2007; 303: 546-553.
    • (2007) J Cryst Growth. , vol.303 , pp. 546-553
    • Blouwolff, J.1    Fraden, S.2
  • 21
    • 0035502143 scopus 로고    scopus 로고
    • Interactions in solution and crystallization of Aspergillus flavus urate oxidase
    • Bonneté F, Vivarès D, Robert C, Colloc'h N. Interactions in solution and crystallization of Aspergillus flavus urate oxidase. J Cryst Growth. 2001; 232: 330-339.
    • (2001) J Cryst Growth. , vol.232 , pp. 330-339
    • Bonneté, F.1    Vivarès, D.2    Robert, C.3    Colloc'h, N.4
  • 22
    • 4344704198 scopus 로고    scopus 로고
    • Predictive models for protein crystallization
    • (San Diego).
    • Rupp B, Wang J. Predictive models for protein crystallization. Methods (San Diego). 2004; 34: 390-407.
    • (2004) Methods , vol.34 , pp. 390-407
    • Rupp, B.1    Wang, J.2
  • 26
    • 33644962807 scopus 로고    scopus 로고
    • A microfluidic device for kinetic optimization of protein crystallization and in situ structure determination
    • Hansen CL, Classen S, Berger JM, Quake SR. A microfluidic device for kinetic optimization of protein crystallization and in situ structure determination. J Am Chem Soc. 2006; 128: 3142-3143.
    • (2006) J Am Chem Soc. , vol.128 , pp. 3142-3143
    • Hansen, C.L.1    Classen, S.2    Berger, J.M.3    Quake, S.R.4
  • 27
    • 0037392925 scopus 로고    scopus 로고
    • High-throughput protein crystallization
    • Hui R, Edwards A. High-throughput protein crystallization. J Struct Biol. 2003; 142: 154-161.
    • (2003) J Struct Biol. , vol.142 , pp. 154-161
    • Hui, R.1    Edwards, A.2
  • 28
    • 33847250908 scopus 로고    scopus 로고
    • Prediction of protein crystallization using collocation of amino acid pairs
    • Chen K, Kurgan L, Rahbari M. Prediction of protein crystallization using collocation of amino acid pairs. Biochem Biophys Res Commun. 2007; 355: 764-769.
    • (2007) Biochem Biophys Res Commun. , vol.355 , pp. 764-769
    • Chen, K.1    Kurgan, L.2    Rahbari, M.3
  • 31
    • 41349121172 scopus 로고    scopus 로고
    • ParCrys: a Parzen window density estimation approach to protein crystallization propensity prediction
    • Overton IM, Padovani G, Girolami MA, Barton GJ. ParCrys: a Parzen window density estimation approach to protein crystallization propensity prediction. Bioinformatics. 2008; 24: 901-907.
    • (2008) Bioinformatics. , vol.24 , pp. 901-907
    • Overton, I.M.1    Padovani, G.2    Girolami, M.A.3    Barton, G.J.4
  • 32
    • 4644311920 scopus 로고    scopus 로고
    • Average protein density is a molecular-weight-dependent function
    • Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function. Protein Sci. 2004; 13: 2825-2828.
    • (2004) Protein Sci. , vol.13 , pp. 2825-2828
    • Fischer, H.1    Polikarpov, I.2    Craievich, A.F.3
  • 34
    • 13444295847 scopus 로고    scopus 로고
    • Crystallization of proteins
    • In Myerson A, editor., 2nd ed., Newton, MA: Butterworth-Heinemann.
    • Wiencek J, Crystallization of proteins. In Myerson A, editor. Handbook of Industrial Crystallization, 2nd ed., Newton, MA: Butterworth-Heinemann; 2002.
    • (2002) Handbook of Industrial Crystallization
    • Wiencek, J.1
  • 35
    • 79961028212 scopus 로고    scopus 로고
    • Methods for reducing or preventing liquid-liquid phase separation in high concentration protein solutions. PCT/US2007/013747
    • Li L, Kantor A, Warne NW. Methods for reducing or preventing liquid-liquid phase separation in high concentration protein solutions. PCT/US2007/013747, 2007.
    • (2007)
    • Li, L.1    Kantor, A.2    Warne, N.W.3
  • 36
    • 0037263109 scopus 로고    scopus 로고
    • Ergodic and non-ergodic phase transitions in globular protein suspensions
    • Kulkarni AM, Dixit NM, Zukoski CF. Ergodic and non-ergodic phase transitions in globular protein suspensions. Faraday Discuss. 2003; 123: 37-50.
    • (2003) Faraday Discuss. , vol.123 , pp. 37-50
    • Kulkarni, A.M.1    Dixit, N.M.2    Zukoski, C.F.3
  • 37
    • 0000478452 scopus 로고    scopus 로고
    • A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
    • Malfois M, Bonnete F, Belloni L, Tardieu A. A model of attractive interactions to account for fluid-fluid phase separation of protein solutions. J Chem Phys. 1996; 105: 3290-3300.
    • (1996) J Chem Phys. , vol.105 , pp. 3290-3300
    • Malfois, M.1    Bonnete, F.2    Belloni, L.3    Tardieu, A.4
  • 45
    • 0028846780 scopus 로고
    • Crystallization of intact monoclonal antibodies
    • Harris LJ, Skaletsky E, McPherson A. Crystallization of intact monoclonal antibodies. Proteins. 1995; 23: 285-289.
    • (1995) Proteins. , vol.23 , pp. 285-289
    • Harris, L.J.1    Skaletsky, E.2    McPherson, A.3
  • 46
    • 0035502093 scopus 로고    scopus 로고
    • The liquid protein phase in crystallization: a case study-intact immunoglobulins
    • Kuznetsov YG, Malkin AJ, McPherson A. The liquid protein phase in crystallization: a case study-intact immunoglobulins. J Cryst Growth. 2001; 232: 30-39.
    • (2001) J Cryst Growth. , vol.232 , pp. 30-39
    • Kuznetsov, Y.G.1    Malkin, A.J.2    McPherson, A.3
  • 48
    • 40849083446 scopus 로고    scopus 로고
    • Effects of pH on protein-protein interactions and implications for protein phase behavior
    • Dumetz AC, Chockla AM, Kaler EW, Lenhoff AM. Effects of pH on protein-protein interactions and implications for protein phase behavior. Biochim Biophys Acta. 2008; 1784: 600-610.
    • (2008) Biochim Biophys Acta. , vol.1784 , pp. 600-610
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 49
    • 0002934030 scopus 로고
    • Studies in the physical chemistry of the proteins. X. The solubility of hemoglobin in solution of chlorides and sulfates of varying concentration
    • Green AA. Studies in the physical chemistry of the proteins. X. The solubility of hemoglobin in solution of chlorides and sulfates of varying concentration. J Biol Chem. 1932; 95: 47-66.
    • (1932) J Biol Chem. , vol.95 , pp. 47-66
    • Green, A.A.1


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