메뉴 건너뛰기




Volumn 27, Issue 5, 2011, Pages 1306-1314

Dual salt precipitation for the recovery of a recombinant protein from Escherichia coli

Author keywords

Dual salt precipitation; Fab; Primary recovery; Scale down centrifugation; Synergistic effects

Indexed keywords

ALTERNATIVE PROCESS; AMMONIUM SULFATE; ANTAGONISTIC EFFECTS; BIOPHARMACEUTICALS; CITRATE IONS; CLARIFICATION PERFORMANCE; FAB; INTRACELLULAR PROTEINS; PRECIPITATING AGENTS; RECOMBINANT PROTEIN; SALT PRECIPITATION; SALTING-OUT EFFECT; SCALE-DOWN; SODIUM CITRATE; SOLUBILITY STUDIES; SYNERGISTIC EFFECT;

EID: 80053929111     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.645     Document Type: Article
Times cited : (11)

References (31)
  • 2
    • 4644309963 scopus 로고    scopus 로고
    • Production technologies for monoclonal antibodies and their fragments
    • Andersen DC, Reilly DE. Production technologies for monoclonal antibodies and their fragments. Curr Opin Biotechnol. 2004; 15: 456-462.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 456-462
    • Andersen, D.C.1    Reilly, D.E.2
  • 3
    • 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
  • 4
    • 33847793307 scopus 로고    scopus 로고
    • Future of antibody purification
    • Low D, O'Leary R, Pujar NS. Future of antibody purification. J Chrom B. 2007; 848: 48-63.
    • (2007) J Chrom B , vol.848 , pp. 48-63
    • Low, D.1    O'Leary, R.2    Pujar, N.S.3
  • 5
    • 0024834497 scopus 로고
    • Purification of IgG from serum with caprylic acid and ammonium sulfate precipitation is not superior to ammonium sulfate precipitation alone
    • Mohanty JG, Elazhary Y. Purification of IgG from serum with caprylic acid and ammonium sulfate precipitation is not superior to ammonium sulfate precipitation alone. Comp lmmun Microb Inject Dis. 1989; 12: 153-160.
    • (1989) Comp lmmun Microb Inject Dis , vol.12 , pp. 153-160
    • Mohanty, J.G.1    Elazhary, Y.2
  • 6
    • 60549099544 scopus 로고    scopus 로고
    • Selective antibody precipitation using polyelectrolytes: a novel approach to the purification of monoclonal antibodies
    • McDonald P, Victa C, Carter-Franklin JN, Fahrner R. Selective antibody precipitation using polyelectrolytes: a novel approach to the purification of monoclonal antibodies. Biotechnol Bioeng. 2009; 102: 1141-1151.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1141-1151
    • McDonald, P.1    Victa, C.2    Carter-Franklin, J.N.3    Fahrner, R.4
  • 7
    • 56449122218 scopus 로고    scopus 로고
    • Selective precipitation-assisted recovery of immunoglobulins from bovine serum using controlled-fouling crossflow membrane microfiltration
    • Venkiteshwaran A, Heider P, Teysseyre L, Belfort G. Selective precipitation-assisted recovery of immunoglobulins from bovine serum using controlled-fouling crossflow membrane microfiltration. Biotechnol Bioeng. 2008; 101: 957-966.
    • (2008) Biotechnol Bioeng , vol.101 , pp. 957-966
    • Venkiteshwaran, A.1    Heider, P.2    Teysseyre, L.3    Belfort, G.4
  • 8
    • 4043162084 scopus 로고    scopus 로고
    • Purification of antibody and antibody-fragment from E. coli homogenate using 6,9-diamino-2-ethoxyacridine lactate as precipitation agent
    • Persson J, Lester P. Purification of antibody and antibody-fragment from E. coli homogenate using 6, 9-diamino-2-ethoxyacridine lactate as precipitation agent. Biotechnol Bioeng. 2004; 87: 424-434.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 424-434
    • Persson, J.1    Lester, P.2
  • 9
    • 0025700878 scopus 로고
    • A new biochemical engineering approach to the fractional precipitation of proteins
    • Richardson P, Hoare M, Dunnill P. A new biochemical engineering approach to the fractional precipitation of proteins. Biotechnol Bioeng. 1990; 36: 354-366.
    • (1990) Biotechnol Bioeng , vol.36 , pp. 354-366
    • Richardson, P.1    Hoare, M.2    Dunnill, P.3
  • 10
    • 0034233433 scopus 로고    scopus 로고
    • Selective flocculation and precipitation for the improvement of virus-like particle recovery from yeast homogenate
    • Tsoka S, Ciniawskyj OC, Thomas OR, Titchener-Hooker NJ, Hoare M. Selective flocculation and precipitation for the improvement of virus-like particle recovery from yeast homogenate. Biotechnol Prog. 2000; 16: 661-667.
    • (2000) Biotechnol Prog , vol.16 , pp. 661-667
    • Tsoka, S.1    Ciniawskyj, O.C.2    Thomas, O.R.3    Titchener-Hooker, N.J.4    Hoare, M.5
  • 12
    • 67650831958 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography in dual salt system increases protein binding capacity
    • Senczuk AM, Klinke R, Arakawa T, Vedantham G, Yigzaw Y. Hydrophobic interaction chromatography in dual salt system increases protein binding capacity. Biotechnol Bioeng. 2009; 103: 930-935.
    • (2009) Biotechnol Bioeng , vol.103 , pp. 930-935
    • Senczuk, A.M.1    Klinke, R.2    Arakawa, T.3    Vedantham, G.4    Yigzaw, Y.5
  • 14
    • 0017288609 scopus 로고
    • The kinetics of protein salting-out: precipitation of yeast enzymes by ammonium sulfate
    • Foster PR, Dunnill P, Lilly MD. The kinetics of protein salting-out: precipitation of yeast enzymes by ammonium sulfate. Biotechnol Bioeng. 1976; 18: 545-580.
    • (1976) Biotechnol Bioeng , vol.18 , pp. 545-580
    • Foster, P.R.1    Dunnill, P.2    Lilly, M.D.3
  • 15
    • 80053904798 scopus 로고
    • The solubility of the plasma proteins: I. Dependence of salt and plasma concentrations in concentrated solutions of potassium phosphate
    • Butler M, Montgomery H. The solubility of the plasma proteins: I. Dependence of salt and plasma concentrations in concentrated solutions of potassium phosphate. J Biol Chem. 1932; 99: 173-195.
    • (1932) J Biol Chem , vol.99 , pp. 173-195
    • Butler, M.1    Montgomery, H.2
  • 16
    • 0034237421 scopus 로고    scopus 로고
    • Buffer effects on the zeta potential of ultrafiltration membranes
    • Burns DB, Zydney AL. Buffer effects on the zeta potential of ultrafiltration membranes. J Memb Sci. 2000; 172: 39-48.
    • (2000) J Memb Sci , vol.172 , pp. 39-48
    • Burns, D.B.1    Zydney, A.L.2
  • 17
    • 33845409018 scopus 로고    scopus 로고
    • A methodology for centrifuge selection for the separation of high solids density cell broths by visualization of performance using windows of operation
    • Salte H, King JMP, Baganz F, Hoare M, Titchener-Hooker NJ. A methodology for centrifuge selection for the separation of high solids density cell broths by visualization of performance using windows of operation. Biotechnol Bioeng. 2006; 95: 1218-1227.
    • (2006) Biotechnol Bioeng , vol.95 , pp. 1218-1227
    • Salte, H.1    King, J.M.P.2    Baganz, F.3    Hoare, M.4    Titchener-Hooker, N.J.5
  • 18
    • 33749364369 scopus 로고    scopus 로고
    • Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification
    • Hutchinson N, Bingham N, Murrell N, Farid S, Hoare M. Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification. Biotechnol Bioeng. 2006; 95: 483-491.
    • (2006) Biotechnol Bioeng , vol.95 , pp. 483-491
    • Hutchinson, N.1    Bingham, N.2    Murrell, N.3    Farid, S.4    Hoare, M.5
  • 20
    • 0034609030 scopus 로고    scopus 로고
    • Laboratory scale-down of protein purification processes involving fractional precipitation and centrifugal recovery
    • Boychyn M, Doyle W, Bulmer M, More J, Hoare M. Laboratory scale-down of protein purification processes involving fractional precipitation and centrifugal recovery. Biotechnol Bioeng. 2000; 69: 1-10.
    • (2000) Biotechnol Bioeng , vol.69 , pp. 1-10
    • Boychyn, M.1    Doyle, W.2    Bulmer, M.3    More, J.4    Hoare, M.5
  • 21
    • 0024397434 scopus 로고
    • Cryocrystalglobulinemia: pH-dependent precipitation of a monoclonal IgG-kappa-immunoglobulin
    • Schoengen A, Schreiner T, Anselstetter V, Binder T, Galle J, Weber L, Heimpel H. Cryocrystalglobulinemia: pH-dependent precipitation of a monoclonal IgG-kappa-immunoglobulin. Blut. 1989; 58: 255-260.
    • (1989) Blut , vol.58 , pp. 255-260
    • Schoengen, A.1    Schreiner, T.2    Anselstetter, V.3    Binder, T.4    Galle, J.5    Weber, L.6    Heimpel, H.7
  • 22
    • 67650692398 scopus 로고    scopus 로고
    • Step change in the efficiency of centrifugation through cell engineering: co-expression of Staphylococcal nuclease to reduce the viscosity of the bioprocess feedstock
    • Balasundaram B, Nesbeth D, Ward JM, Bracewell DG. Step change in the efficiency of centrifugation through cell engineering: co-expression of Staphylococcal nuclease to reduce the viscosity of the bioprocess feedstock. Biotechnol Bioeng. 2009; 104: 134-142.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 134-142
    • Balasundaram, B.1    Nesbeth, D.2    Ward, J.M.3    Bracewell, D.G.4
  • 23
    • 42049107042 scopus 로고    scopus 로고
    • Ultra scale-down to define and improve the relationship between flocculation and disc-stack centrifugation
    • Berrill A, Ho SV, Bracewell DG. Ultra scale-down to define and improve the relationship between flocculation and disc-stack centrifugation. Biotechnol Prog. 2008; 24: 426-431.
    • (2008) Biotechnol Prog , vol.24 , pp. 426-431
    • Berrill, A.1    Ho, S.V.2    Bracewell, D.G.3
  • 24
    • 0037454676 scopus 로고    scopus 로고
    • An ultra scale-down approach for the prediction of full-scale recovery of ovine polyclonal immunoglobulins used in the manufacture of snake venom-specific Fab' fragment
    • Neal G, Christie J, Ayazi-Shamlou P, Keshavarz-Moore E. An ultra scale-down approach for the prediction of full-scale recovery of ovine polyclonal immunoglobulins used in the manufacture of snake venom-specific Fab' fragment. Biotechnol Bioeng. 2003; 81: 149-157.
    • (2003) Biotechnol Bioeng , vol.81 , pp. 149-157
    • Neal, G.1    Christie, J.2    Ayazi-Shamlou, P.3    Keshavarz-Moore, E.4
  • 25
    • 73249147912 scopus 로고    scopus 로고
    • Ultra scale-down approaches for clarification of mammalian cell culture broths in disc-stack centrifuges
    • Zaman F, Allan CM, Ho SV. Ultra scale-down approaches for clarification of mammalian cell culture broths in disc-stack centrifuges. Biotechnol Prog. 2009; 25: 1709-1716.
    • (2009) Biotechnol Prog , vol.25 , pp. 1709-1716
    • Zaman, F.1    Allan, C.M.2    Ho, S.V.3
  • 26
    • 0030049916 scopus 로고    scopus 로고
    • Pilot-scale verification of a computer-based simulation for the centrifugal recovery of biological particles
    • Clarkson AI, Bulmer M, Titchener-Hooker NJ. Pilot-scale verification of a computer-based simulation for the centrifugal recovery of biological particles. Bioprocess Eng. 1996; 14: 81-89.
    • (1996) Bioprocess Eng , vol.14 , pp. 81-89
    • Clarkson, A.I.1    Bulmer, M.2    Titchener-Hooker, N.J.3
  • 27
    • 0017623134 scopus 로고
    • Salt effects on hydropobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic sereies
    • Melander W, Horvath C. Salt effects on hydropobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic sereies. Arch Biochem Biophys. 1977; 183: 200-215.
    • (1977) Arch Biochem Biophys , vol.183 , pp. 200-215
    • Melander, W.1    Horvath, C.2
  • 28
    • 65349103957 scopus 로고    scopus 로고
    • Small molecule clearance in ultrafiltration/diafiltration in relation to protein interactions: study of citrate binding to a Fab
    • Harinarayan C, Skidmore K, Kao Y, Zydney L, van Reis R. Small molecule clearance in ultrafiltration/diafiltration in relation to protein interactions: study of citrate binding to a Fab. Biotechnol Bioeng. 2009; 102: 1718-1722.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1718-1722
    • Harinarayan, C.1    Skidmore, K.2    Kao, Y.3    Zydney, L.4    van Reis, R.5
  • 29
    • 0027113003 scopus 로고
    • Some characteristics of protein precipitation by salts
    • Shih YC, Prausnitz JM, Blanch HW. Some characteristics of protein precipitation by salts. Biotechnol Bioeng. 1992; 40: 1155-1164.
    • (1992) Biotechnol Bioeng , vol.40 , pp. 1155-1164
    • Shih, Y.C.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 30
    • 0028372337 scopus 로고
    • Protein precipitation: effects of mixing on protein solubility
    • Iyer HV, Przybycien TM. Protein precipitation: effects of mixing on protein solubility. AIChE J. 1994; 40: 349-360.
    • (1994) AIChE J , vol.40 , pp. 349-360
    • Iyer, H.V.1    Przybycien, T.M.2
  • 31
    • 0028725645 scopus 로고    scopus 로고
    • Purification of antibodies using ammonium sulfate fractionation or gel filtration. Immunocytochemical methods and protocols
    • Kent UM. Purification of antibodies using ammonium sulfate fractionation or gel filtration. Immunocytochemical methods and protocols. Methods Mol Biol. 1999; 34: 13-21.
    • (1999) Methods Mol Biol , vol.34 , pp. 13-21
    • Kent, U.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.