메뉴 건너뛰기




Volumn 130, Issue , 2014, Pages 45-55

Effect of phase inversion and separation on hepatitis B core antigen extraction from unclarified bacterial feedstock using aqueous two-phase system

Author keywords

Aqueous two phase system; Hepatitis B core antigen; Phase separation; Protein purification

Indexed keywords

ANTIGENS; CENTRIFUGATION; ESCHERICHIA COLI; FEEDSTOCKS; PHASE DIAGRAMS; PLANTS (BOTANY); PROTEINS; PURIFICATION; RECOVERY; SIZE EXCLUSION CHROMATOGRAPHY; SUGAR (SUCROSE);

EID: 84899861748     PISSN: 13835866     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.seppur.2014.04.017     Document Type: Article
Times cited : (5)

References (89)
  • 1
    • 0024237624 scopus 로고
    • Identification of a major hepatitis B core antigen (HBcAg) determinant by using synthetic peptides and monoclonal antibodies
    • G. Colucci, Y. Beazer, C. Cantaluppi, and C. Tackney Identification of a major hepatitis B core antigen (HBcAg) determinant by using synthetic peptides and monoclonal antibodies J. Immunol. 141 1985 4376 4380
    • (1985) J. Immunol. , vol.141 , pp. 4376-4380
    • Colucci, G.1    Beazer, Y.2    Cantaluppi, C.3    Tackney, C.4
  • 2
    • 0020316090 scopus 로고
    • Electron microscopy of hepatitis B core antigen synthesized in E. Coli
    • B.J. Cohen, and J.E. Richmond Electron microscopy of hepatitis B core antigen synthesized in E. coli Nature 296 1982 277 278
    • (1982) Nature , vol.296 , pp. 277-278
    • Cohen, B.J.1    Richmond, J.E.2
  • 3
    • 37549001311 scopus 로고    scopus 로고
    • Expression and purification of the recombinant HBcAg core particles derived from methyltrophic Pichia pastoris, and TEM and AFM of the core particles and their natural aggregates
    • H. Chen Expression and purification of the recombinant HBcAg core particles derived from methyltrophic Pichia pastoris, and TEM and AFM of the core particles and their natural aggregates J. Electron. Microsc. (Tokyo) 56 2007 235 242
    • (2007) J. Electron. Microsc. (Tokyo) , vol.56 , pp. 235-242
    • Chen, H.1
  • 4
    • 0032928864 scopus 로고    scopus 로고
    • Hepatitis B core particles as a universal display model: A structure-function basis for development
    • P. Pumpens, and E. Grens Hepatitis B core particles as a universal display model: a structure-function basis for development Hepatitis FEBS Lett. 442 1999 1 6
    • (1999) Hepatitis FEBS Lett. , vol.442 , pp. 1-6
    • Pumpens, P.1    Grens, E.2
  • 5
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • R.A. Crowther, N.A. Kiseley, B. Böttcher, J.A. Berriman, G.P. Borisova, and V. Ose et al. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy Cell 77 1994 943 950
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiseley, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6
  • 6
    • 0344199395 scopus 로고    scopus 로고
    • New chimaeric hepatitis B virus core particles carrying Hantavirus (serotype Puumala) epitopes: Immunogenicity and protection against virus challenge
    • R. Ulrich, D. Koletzki, S. Lachmann, A. Lundkvist, A. Zankl, and A. Kazaks et al. New chimaeric hepatitis B virus core particles carrying Hantavirus (serotype Puumala) epitopes: immunogenicity and protection against virus challenge J. Biotechnol. 73 1999 141 153
    • (1999) J. Biotechnol. , vol.73 , pp. 141-153
    • Ulrich, R.1    Koletzki, D.2    Lachmann, S.3    Lundkvist, A.4    Zankl, A.5    Kazaks, A.6
  • 7
    • 0030608502 scopus 로고    scopus 로고
    • Expression of a human cytomegalovirus gp58 antigenic domain fused to the hepatitis B virus nucleocapsid protein
    • M.R. Tarar, V.C. Emery, and T.J. Harrison Expression of a human cytomegalovirus gp58 antigenic domain fused to the hepatitis B virus nucleocapsid protein FEMS Immunol. Med. Microbiol. 16 1996 183 192
    • (1996) FEMS Immunol. Med. Microbiol. , vol.16 , pp. 183-192
    • Tarar, M.R.1    Emery, V.C.2    Harrison, T.J.3
  • 8
    • 0028842722 scopus 로고
    • Theileria annulata sporozoite antigen fused to hepatitis B core antigen used in a vaccination trial
    • N.R. Boulter, E.J. Glass, P.A. Knight, L. Bell-Sakyi, C.G. Duncan Brown, and R. Hall Theileria annulata sporozoite antigen fused to hepatitis B core antigen used in a vaccination trial Vaccine 13 1995 1152 1160
    • (1995) Vaccine , vol.13 , pp. 1152-1160
    • Boulter, N.R.1    Glass, E.J.2    Knight, P.A.3    Bell-Sakyi, L.4    Duncan Brown, C.G.5    Hall, R.6
  • 9
    • 33846240816 scopus 로고    scopus 로고
    • Advantages to the use of rodent hepadnavirus core proteins as vaccine platforms
    • J.N. Billaud, D. Peterson, B.O. Lee, T. Maruyama, A. Chen, and M. Sallberg et al. Advantages to the use of rodent hepadnavirus core proteins as vaccine platforms Vaccine 25 2007 1593 1606
    • (2007) Vaccine , vol.25 , pp. 1593-1606
    • Billaud, J.N.1    Peterson, D.2    Lee, B.O.3    Maruyama, T.4    Chen, A.5    Sallberg, M.6
  • 10
    • 36148964724 scopus 로고    scopus 로고
    • Interactions of hepatitis B core antigen and peptide inhibitors
    • K.F. Tang, M.P. Abdullah, K. Yusoff, and W.S. Tan Interactions of hepatitis B core antigen and peptide inhibitors J. Med. Chem. 50 2007 5620 5626
    • (2007) J. Med. Chem. , vol.50 , pp. 5620-5626
    • Tang, K.F.1    Abdullah, M.P.2    Yusoff, K.3    Tan, W.S.4
  • 12
    • 33344479476 scopus 로고    scopus 로고
    • Rapid, high-level production of hepatitis B core antigen in plant leaf and its immunogenicity in mice
    • Z. Huang, L. Santi, K. LePore, J. Kilbourne, C.J. Arntzen, and H.S. Mason Rapid, high-level production of hepatitis B core antigen in plant leaf and its immunogenicity in mice Vaccine 24 2006 2506 2513
    • (2006) Vaccine , vol.24 , pp. 2506-2513
    • Huang, Z.1    Santi, L.2    Lepore, K.3    Kilbourne, J.4    Arntzen, C.J.5    Mason, H.S.6
  • 13
    • 0038405161 scopus 로고    scopus 로고
    • Hepatitis B virus core antigen: Enhancement of its production in Escherichia coli, and interaction of the core particles with the viral surface antigen
    • W.S. Tan, M.R. Dyson, and K. Murray Hepatitis B virus core antigen: enhancement of its production in Escherichia coli, and interaction of the core particles with the viral surface antigen Biol. Chem. 384 2003 363 371
    • (2003) Biol. Chem. , vol.384 , pp. 363-371
    • Tan, W.S.1    Dyson, M.R.2    Murray, K.3
  • 14
    • 28944455694 scopus 로고    scopus 로고
    • Affinity chromatography matures as bioinformatic and combinatorial tools develop
    • Y.D. Clonis Affinity chromatography matures as bioinformatic and combinatorial tools develop J. Chromatogr. A 1101 2006 1 24
    • (2006) J. Chromatogr. A , vol.1101 , pp. 1-24
    • Clonis, Y.D.1
  • 15
    • 0031172715 scopus 로고    scopus 로고
    • Expanded-bed adsorption in industrial bioprocessing: Recent developments
    • R. Hjorth Expanded-bed adsorption in industrial bioprocessing: recent developments Trends Biotechnol. 15 1997 230 235
    • (1997) Trends Biotechnol. , vol.15 , pp. 230-235
    • Hjorth, R.1
  • 16
    • 0036664984 scopus 로고    scopus 로고
    • Purification of the recombinant hepatitis B core antigen, and its potential use for the diagnosis of Hepatitis B virus infection
    • D.O. Palenzuela, L. Núñez, J. Roca, B. Acevedo, T. Diaz, J. Benitez, and J.V. Gavilondo Purification of the recombinant hepatitis B core antigen, and its potential use for the diagnosis of Hepatitis B virus infection Biotechnol. Appl. 19 2002 138 142
    • (2002) Biotechnol. Appl. , vol.19 , pp. 138-142
    • Palenzuela, D.O.1    Núñez, L.2    Roca, J.3    Acevedo, B.4    Diaz, T.5    Benitez, J.6    Gavilondo, J.V.7
  • 17
    • 0005166241 scopus 로고    scopus 로고
    • Aqueous two phase systems: An attractive technology for downstream processing of biomolecules
    • R. Gupta, S. Bradoo, and R.K. Saxena Aqueous two phase systems: an attractive technology for downstream processing of biomolecules Curr. Prot. Pept. Sci. 77 1999 520 523
    • (1999) Curr. Prot. Pept. Sci. , vol.77 , pp. 520-523
    • Gupta, R.1    Bradoo, S.2    Saxena, R.K.3
  • 18
    • 0034468008 scopus 로고    scopus 로고
    • Recovery of endo-polygalacturonase using polyethylene glycol-salt aqueous two-phase extraction with polymer recycling
    • Y.T. Wu, M. Pereira, A. Venancio, and J. Texeira Recovery of endo-polygalacturonase using polyethylene glycol-salt aqueous two-phase extraction with polymer recycling Bioseparation 9 2000 247 254
    • (2000) Bioseparation , vol.9 , pp. 247-254
    • Wu, Y.T.1    Pereira, M.2    Venancio, A.3    Texeira, J.4
  • 19
    • 0020783232 scopus 로고
    • A process for large scale isolation of β-galactosidase from E. Coli in an aqueous two-phase system
    • A. Velde, A.L. Smeds, and S.O. Enfors A process for large scale isolation of β-galactosidase from E. coli in an aqueous two-phase system Biotechnol. Bioeng. 25 1983 1789 1800
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 1789-1800
    • Velde, A.1    Smeds, A.L.2    Enfors, S.O.3
  • 20
    • 0000528129 scopus 로고
    • Aqueous two-phase systems
    • Academic Press New York
    • H. Walter, and G. Johansson Aqueous two-phase systems Methods in Enzymology 1994 Academic Press New York 228
    • (1994) Methods in Enzymology , pp. 228
    • Walter, H.1    Johansson, G.2
  • 23
    • 62049083384 scopus 로고    scopus 로고
    • Recovery of laccase from the residual compost of Agaricus biporus in aqueous two-phase system
    • K. Mayolo-Deloisa, M.D.R. Trejo-Hernindez, and M. Rito-Palomares Recovery of laccase from the residual compost of Agaricus biporus in aqueous two-phase system Process Biochem. 44 2009 435 439
    • (2009) Process Biochem. , vol.44 , pp. 435-439
    • Mayolo-Deloisa, K.1    Trejo-Hernindez, M.D.R.2    Rito-Palomares, M.3
  • 24
    • 0033813583 scopus 로고    scopus 로고
    • Fermentation and downstream processing of lipase from Aspergillus terreus
    • R. Gulati, R.K. Saxena, and R. Gupta Fermentation and downstream processing of lipase from Aspergillus terreus Process Biochem. 36 2000 149 155
    • (2000) Process Biochem. , vol.36 , pp. 149-155
    • Gulati, R.1    Saxena, R.K.2    Gupta, R.3
  • 25
    • 0348110469 scopus 로고    scopus 로고
    • Extraction of plasmid DNA from E. Coli cell lysate in a thermo-separating aqueous two-phase system
    • C. Kepka, J. Rhodin, R. Lemmens, F. Tjerneld, and P.E. Gustavsson Extraction of plasmid DNA from E. coli cell lysate in a thermo-separating aqueous two-phase system J. Chromatogr. A 1024 2004 95 104
    • (2004) J. Chromatogr. A , vol.1024 , pp. 95-104
    • Kepka, C.1    Rhodin, J.2    Lemmens, R.3    Tjerneld, F.4    Gustavsson, P.E.5
  • 26
    • 2342538394 scopus 로고    scopus 로고
    • Partitioning behavior of amino acids in aqueous two-phase systems containing polyethylene glycol and phosphate buffer
    • Q.K. Shang, W. Li, Q. Jia, and D.Q. Li Partitioning behavior of amino acids in aqueous two-phase systems containing polyethylene glycol and phosphate buffer Fluid Phase Equilibr. 219 2004 195 203
    • (2004) Fluid Phase Equilibr. , vol.219 , pp. 195-203
    • Shang, Q.K.1    Li, W.2    Jia, Q.3    Li, D.Q.4
  • 27
    • 77950101404 scopus 로고    scopus 로고
    • Aqueous two-phase systems: A viable platform in the manufacturing of biopharmaceuticals
    • P.A.J. Rosa, I.F. Ferreira, A.M. Azevedo, and M.R. Aires-Barros Aqueous two-phase systems: a viable platform in the manufacturing of biopharmaceuticals J. Chromatogr. A 1217 2010 2296 2305
    • (2010) J. Chromatogr. A , vol.1217 , pp. 2296-2305
    • Rosa, P.A.J.1    Ferreira, I.F.2    Azevedo, A.M.3    Aires-Barros, M.R.4
  • 28
    • 29244459159 scopus 로고    scopus 로고
    • Partitioning and purification of lysozyme from chicken egg white using aqueous two-phase system
    • C.K. Su, and B.H. Chiang Partitioning and purification of lysozyme from chicken egg white using aqueous two-phase system Process Biochem. 41 2009 257 263
    • (2009) Process Biochem. , vol.41 , pp. 257-263
    • Su, C.K.1    Chiang, B.H.2
  • 29
    • 33747883548 scopus 로고    scopus 로고
    • Development of an aqueous two-phase partitioning system for fractionating therapeutic proteins from tobacco extract
    • D. Platis, and N.E. Labrou Development of an aqueous two-phase partitioning system for fractionating therapeutic proteins from tobacco extract J. Chromatogr. A 1128 2006 114 124
    • (2006) J. Chromatogr. A , vol.1128 , pp. 114-124
    • Platis, D.1    Labrou, N.E.2
  • 30
    • 84860498520 scopus 로고    scopus 로고
    • Recovery of biological products in aqueous two-phase systems
    • K. Ratanapongleka Recovery of biological products in aqueous two-phase systems Int. J. Chem. Eng. Appl. 1 2010 191 197
    • (2010) Int. J. Chem. Eng. Appl. , vol.1 , pp. 191-197
    • Ratanapongleka, K.1
  • 31
    • 62549139648 scopus 로고    scopus 로고
    • Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing
    • A.M. Azevedo, P.A.J. Rosa, I.F. Ferreira, and M.Q. Aires-Barros Chromatography-free recovery of biopharmaceuticals through aqueous two-phase processing Trends Biotechnol. 27 2009 240 247
    • (2009) Trends Biotechnol. , vol.27 , pp. 240-247
    • Azevedo, A.M.1    Rosa, P.A.J.2    Ferreira, I.F.3    Aires-Barros, M.Q.4
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 35548939928 scopus 로고    scopus 로고
    • Direct purification of recombinant hepatitis B core antigen from two different pre-conditioned unclarified Escherichia coli feedstocks via expanded bed adsorption chromatography
    • M.Y.T. Ng, W.S. Tan, N. Abdullah, T.C. Ling, and B.T. Tey Direct purification of recombinant hepatitis B core antigen from two different pre-conditioned unclarified Escherichia coli feedstocks via expanded bed adsorption chromatography J. Chromatogr. A 1172 2007 47 56
    • (2007) J. Chromatogr. A , vol.1172 , pp. 47-56
    • Ng, M.Y.T.1    Tan, W.S.2    Abdullah, N.3    Ling, T.C.4    Tey, B.T.5
  • 38
    • 84859781333 scopus 로고    scopus 로고
    • Effect of aqueous two-phase system constituents in different poly(ethylene glycol)-salt phase diagrams
    • S.C. Silvério, A. Wegrzyn, E. Lladosa, O. Rodrígurz, and E.A. Macedo Effect of aqueous two-phase system constituents in different poly(ethylene glycol)-salt phase diagrams J. Chem. Eng. Data 57 2012 1203 1208
    • (2012) J. Chem. Eng. Data , vol.57 , pp. 1203-1208
    • Silvério, S.C.1    Wegrzyn, A.2    Lladosa, E.3    Rodrígurz, O.4    Macedo, E.A.5
  • 39
    • 84899798252 scopus 로고    scopus 로고
    • Phase compositions of aqueous two-phase systems formed by poly(ethylene glycol) and maltodextrin at different temperatures
    • D. Ramyadevi, A. Subathira, and S. Saravanan Phase compositions of aqueous two-phase systems formed by poly(ethylene glycol) and maltodextrin at different temperatures Int. J. Chem. Sci. Appl. 3 2012 289 292
    • (2012) Int. J. Chem. Sci. Appl. , vol.3 , pp. 289-292
    • Ramyadevi, D.1    Subathira, A.2    Saravanan, S.3
  • 40
    • 33845880129 scopus 로고    scopus 로고
    • Partition of tannery wastewater proteins in aqueous two-phase poly (ethylene glycol)-magnesium sulphate systems: Effect of molecular weights and pH
    • S. Saravanan, J.R. Rao, T. Murugesan, B.U. Nair, and T. Ramasami Partition of tannery wastewater proteins in aqueous two-phase poly (ethylene glycol)-magnesium sulphate systems: effect of molecular weights and pH Chem. Eng. Sci. 62 2007 969 978
    • (2007) Chem. Eng. Sci. , vol.62 , pp. 969-978
    • Saravanan, S.1    Rao, J.R.2    Murugesan, T.3    Nair, B.U.4    Ramasami, T.5
  • 41
    • 43449104549 scopus 로고    scopus 로고
    • Liquid-liquid equilibria of biphasic systems composed of sodium citrate + polyethylene(glycol) 1500 or 4000 at different temperatures
    • R.M. De Oliveira, J.R. Coimbra, L.A. Minim, L.H.M. da Silva, and M.P.F. Fontes Liquid-liquid equilibria of biphasic systems composed of sodium citrate + polyethylene(glycol) 1500 or 4000 at different temperatures J. Chem. Eng. Data 53 2008 895 899
    • (2008) J. Chem. Eng. Data , vol.53 , pp. 895-899
    • De Oliveira, R.M.1    Coimbra, J.R.2    Minim, L.A.3    Da Silva, L.H.M.4    Fontes, M.P.F.5
  • 42
    • 34548046487 scopus 로고    scopus 로고
    • Evaluation of recombinant phenylalanine dehydrogenase behaviour in aqueous two-phase partitioning
    • H.S. Mohamadi, E. Omidinia, and R. Dinarvand Evaluation of recombinant phenylalanine dehydrogenase behaviour in aqueous two-phase partitioning Process Biochem. 42 2007 1296 1301
    • (2007) Process Biochem. , vol.42 , pp. 1296-1301
    • Mohamadi, H.S.1    Omidinia, E.2    Dinarvand, R.3
  • 43
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • K.D. Collins, and M.W. Washabaugh The Hofmeister effect and the behaviour of water at interfaces Q. Rev. Biophys. 18 1985 323 422
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 45
    • 79953313189 scopus 로고    scopus 로고
    • Effect of pH on the phase separation in the ternary aqueous system containing the hydrophilic ionic liquid 1-butyl-3-methylimidazonium bromide and the kosmotropic salt potassium citrate at 298.15 K
    • M.T. Zafarani-Moattar, and S. Hamzehzadeh Effect of pH on the phase separation in the ternary aqueous system containing the hydrophilic ionic liquid 1-butyl-3-methylimidazonium bromide and the kosmotropic salt potassium citrate at 298.15 K Fluid Phase Equilibr. 304 2011 110 120
    • (2011) Fluid Phase Equilibr. , vol.304 , pp. 110-120
    • Zafarani-Moattar, M.T.1    Hamzehzadeh, S.2
  • 47
    • 0037203568 scopus 로고    scopus 로고
    • Amylase partitioning and extractive bioconversion of starch using thermoseparating aqueous two-phase systems
    • M. Li, J.W. Kim, and T.L. Peeples Amylase partitioning and extractive bioconversion of starch using thermoseparating aqueous two-phase systems J. Biotechnol. 93 2002 15 26
    • (2002) J. Biotechnol. , vol.93 , pp. 15-26
    • Li, M.1    Kim, J.W.2    Peeples, T.L.3
  • 48
    • 79951890830 scopus 로고    scopus 로고
    • Liquid-liquid equilibria of aqueous two-phase systems containing polyethylene glycol 4000 and two different salts of ammonium
    • G. Khayati, A. Daghbandan, H. Gilvari, and N. Pheyz-Sani Liquid-liquid equilibria of aqueous two-phase systems containing polyethylene glycol 4000 and two different salts of ammonium Res. J. Appl. Sci. Eng. Tech. 2 2011 96 98
    • (2011) Res. J. Appl. Sci. Eng. Tech. , vol.2 , pp. 96-98
    • Khayati, G.1    Daghbandan, A.2    Gilvari, H.3    Pheyz-Sani, N.4
  • 49
    • 45649083029 scopus 로고    scopus 로고
    • Extraction of metal ions in aqueous polyethylene glycol- inorganic salt two-phase systems in the presence of inorganic extractants: Correlation between extraction behaviour of and stability constants of extracted species
    • L. Bulgariu, and D. Bulgariu Extraction of metal ions in aqueous polyethylene glycol- inorganic salt two-phase systems in the presence of inorganic extractants: correlation between extraction behaviour of and stability constants of extracted species J. Chromatogr. A 1196-1197 2008 117 124
    • (2008) J. Chromatogr. A , vol.1196-1197 , pp. 117-124
    • Bulgariu, L.1    Bulgariu, D.2
  • 50
    • 78651395309 scopus 로고    scopus 로고
    • Salt effect on the aqueous two-phase system PEG 8000-sodium sulphate
    • L.A. Ferreira, and J.A. Teixeira Salt effect on the aqueous two-phase system PEG 8000-sodium sulphate J. Chem. Eng. Data 56 2011 133 137
    • (2011) J. Chem. Eng. Data , vol.56 , pp. 133-137
    • Ferreira, L.A.1    Teixeira, J.A.2
  • 52
    • 77949261437 scopus 로고    scopus 로고
    • Liquid-liquid equilibria of aqueous two-phase systems composed of TritonX-100 and sodium citrate or magnesium sulphate salts
    • A. Salabat, S.T. Moghadam, and M.R. Far Liquid-liquid equilibria of aqueous two-phase systems composed of TritonX-100 and sodium citrate or magnesium sulphate salts CALPHAD 34 2010 81 83
    • (2010) CALPHAD , vol.34 , pp. 81-83
    • Salabat, A.1    Moghadam, S.T.2    Far, M.R.3
  • 53
    • 0015237087 scopus 로고
    • Fractionation of proteins and viruses with polyethylene glycol
    • I.R.M. Juckes Fractionation of proteins and viruses with polyethylene glycol Biochim. Biophys. Acta 229 1971 535 546
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 535-546
    • Juckes, I.R.M.1
  • 54
    • 0031281935 scopus 로고    scopus 로고
    • Three-phase partitioning: Concentration and purification of proteins
    • C. Dennison, and R. Lovrien Three-phase partitioning: concentration and purification of proteins Protein Expres. Purif. 11 1997 149 161
    • (1997) Protein Expres. Purif. , vol.11 , pp. 149-161
    • Dennison, C.1    Lovrien, R.2
  • 56
    • 77952321851 scopus 로고    scopus 로고
    • A descriptive model and methods for up-scaled process routes for interfacial partition of bioparticles in aqueous two-phase systems
    • F. Luechau, T.C. Ling, and A. Lyddiatt A descriptive model and methods for up-scaled process routes for interfacial partition of bioparticles in aqueous two-phase systems Biochem. Eng. J. 50 2010 122 130
    • (2010) Biochem. Eng. J. , vol.50 , pp. 122-130
    • Luechau, F.1    Ling, T.C.2    Lyddiatt, A.3
  • 57
    • 0343336724 scopus 로고
    • Affinity partitioning of biopolymers and membranes in ficoll-dextran aqueous two-phase systems
    • G. Johansson, M. Joelsson, and B. Olde Affinity partitioning of biopolymers and membranes in ficoll-dextran aqueous two-phase systems J. Chromatogr. B 331 1985 11 21
    • (1985) J. Chromatogr. B , vol.331 , pp. 11-21
    • Johansson, G.1    Joelsson, M.2    Olde, B.3
  • 58
    • 55049115983 scopus 로고    scopus 로고
    • Effect of different operating modes and biomass concentrations on the recovery of recombinant hepatitis B core antigen from thermal-treated unclarified Escherichia coli feedstock
    • M.Y.T. Ng, W.S. Tan, N. Abdullah, T.C. Ling, and B.T. Tey Effect of different operating modes and biomass concentrations on the recovery of recombinant hepatitis B core antigen from thermal-treated unclarified Escherichia coli feedstock J. Biotechnol. 138 2008 74 79
    • (2008) J. Biotechnol. , vol.138 , pp. 74-79
    • Ng, M.Y.T.1    Tan, W.S.2    Abdullah, N.3    Ling, T.C.4    Tey, B.T.5
  • 60
    • 84899810050 scopus 로고    scopus 로고
    • Protein aggregation and precipitation, measurement and control
    • M.C. Flickinger, John Wiley and Sons United States
    • C.H. Schein Protein aggregation and precipitation, measurement and control M.C. Flickinger, Downstream Industrial Processing: Recovery and Purification 2013 John Wiley and Sons United States
    • (2013) Downstream Industrial Processing: Recovery and Purification
    • Schein, C.H.1
  • 61
    • 0032569070 scopus 로고    scopus 로고
    • Aqueous-two phase systems for proteins separation studies on phase inversion
    • J.C. Merchuk, B.A. Andrews, and J.A. Asenjo Aqueous-two phase systems for proteins separation studies on phase inversion J. Chromatogr. B 711 1998 285 293
    • (1998) J. Chromatogr. B , vol.711 , pp. 285-293
    • Merchuk, J.C.1    Andrews, B.A.2    Asenjo, J.A.3
  • 62
    • 84859978697 scopus 로고    scopus 로고
    • Aqueous two-phase systems for protein separation and applications
    • J.S. Asenjo, and B.A. Andrews Aqueous two-phase systems for protein separation and applications J. Chromatogr. A 1238 2012 1 10
    • (2012) J. Chromatogr. A , vol.1238 , pp. 1-10
    • Asenjo, J.S.1    Andrews, B.A.2
  • 66
    • 0028783325 scopus 로고
    • Kinetics of phase separation for polyethylene glycol-phosphate two phase systems
    • A. Kaul, R.A. Pereira, J.A. Asenjo, and J.C. Merchuk Kinetics of phase separation for polyethylene glycol-phosphate two phase systems Biotechnol. Bioeng. 48 1995 246 256
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 246-256
    • Kaul, A.1    Pereira, R.A.2    Asenjo, J.A.3    Merchuk, J.C.4
  • 67
    • 15844379578 scopus 로고
    • Influence of engineering variables upon the morphology of filamentous molds
    • J.C. van Suijdam, and B. Metz Influence of engineering variables upon the morphology of filamentous molds Biotechnol. Bioeng. 23 1981 111 148
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 111-148
    • Van Suijdam, J.C.1    Metz, B.2
  • 68
    • 0037142779 scopus 로고    scopus 로고
    • Phase separation rates of aqueous two-phase systems: Correlation with system properties
    • J.A. Asenjo, S.L. Mistry, B.A. Andrews, and J.C. Merchuk Phase separation rates of aqueous two-phase systems: correlation with system properties Biotechnol. Bioeng. 79 2002 217 223
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 217-223
    • Asenjo, J.A.1    Mistry, S.L.2    Andrews, B.A.3    Merchuk, J.C.4
  • 69
    • 0347320731 scopus 로고    scopus 로고
    • Phase equilibrium and insulin partitioning in aqueous two-phase systems containing block copolymers and potassium phosphate
    • L.H. Haraguchi, R.S. Mohamed, W. Loh, and P.A. Pessôa Filho Phase equilibrium and insulin partitioning in aqueous two-phase systems containing block copolymers and potassium phosphate Fluid Phase Equilibr. 215 2004 1 15
    • (2004) Fluid Phase Equilibr. , vol.215 , pp. 1-15
    • Haraguchi, L.H.1    Mohamed, R.S.2    Loh, W.3    Pessôa Filho, P.A.4
  • 71
    • 84945974245 scopus 로고    scopus 로고
    • The effect of sulphates on partitioning of pectinases in aqueous two-phase systems
    • M.G. Antov, M. Peričin, and B.I. Trbojević The effect of sulphates on partitioning of pectinases in aqueous two-phase systems APTEFF 35 2004 179 186
    • (2004) APTEFF , vol.35 , pp. 179-186
    • Antov, M.G.1    Peričin, M.2    Trbojević, B.I.3
  • 72
    • 85101282709 scopus 로고    scopus 로고
    • Phase diagrams of the aqueous two-phase system of poly(ethylene glycol)/sodium polyacrylate/salts
    • H.O. Johansson, E. Feitosa, and A. Pesso Phase diagrams of the aqueous two-phase system of poly(ethylene glycol)/sodium polyacrylate/salts Polymers 3 2011 387 601
    • (2011) Polymers , vol.3 , pp. 387-601
    • Johansson, H.O.1    Feitosa, E.2    Pesso, A.3
  • 73
    • 2642519497 scopus 로고    scopus 로고
    • Recovery in aqueous two-phase systems of lutein produced by the green microalgae
    • M. Cisneros, J. Benavides, C.H. Brenes, and M. Rito-Palomares Recovery in aqueous two-phase systems of lutein produced by the green microalgae J. Chromatogr. B 807 2004 105 111
    • (2004) J. Chromatogr. B , vol.807 , pp. 105-111
    • Cisneros, M.1    Benavides, J.2    Brenes, C.H.3    Rito-Palomares, M.4
  • 75
    • 84864959396 scopus 로고    scopus 로고
    • Aqueous two-phase systems: A new approach for the determination of brilliant blue FCF in water and food samples
    • S. Shiri, T. Khezeli, S. Lofti, and S. Shiri Aqueous two-phase systems: a new approach for the determination of brilliant blue FCF in water and food samples J. Chem. 2013 2013 1 6
    • (2013) J. Chem. , vol.2013 , pp. 1-6
    • Shiri, S.1    Khezeli, T.2    Lofti, S.3    Shiri, S.4
  • 76
    • 0014687858 scopus 로고
    • Large-scale preparations of viruses by steric chromatography on columns of controlled pore glass: øx174, M13, M12, Qβ and T4 bacteriophages
    • H.H. Gschwender, W. Haller, and P.H. Hofschneider Large-scale preparations of viruses by steric chromatography on columns of controlled pore glass: øx174, M13, M12, Qβ and T4 bacteriophages Biochim. Biophys. Acta 190 1969 460 469
    • (1969) Biochim. Biophys. Acta , vol.190 , pp. 460-469
    • Gschwender, H.H.1    Haller, W.2    Hofschneider, P.H.3
  • 78
    • 0030636302 scopus 로고    scopus 로고
    • Inclusion bodies and purification of proteins in biologically active forms
    • A. Mukhopadhyay Inclusion bodies and purification of proteins in biologically active forms Adv. Biochem. Eng./Biotechnol. 56 1997 61 109
    • (1997) Adv. Biochem. Eng./Biotechnol. , vol.56 , pp. 61-109
    • Mukhopadhyay, A.1
  • 79
    • 84899810510 scopus 로고    scopus 로고
    • Partitioning of plasmid DNA in polymer-salt two-phase systems
    • F. Luechau, T.C. Ling, and A. Lyddiatt Partitioning of plasmid DNA in polymer-salt two-phase systems Sep. Purif. Technol. 66 2009 43 61
    • (2009) Sep. Purif. Technol. , vol.66 , pp. 43-61
    • Luechau, F.1    Ling, T.C.2    Lyddiatt, A.3
  • 81
    • 0003425162 scopus 로고
    • H. Walter, D.E. Brooks, D. Fisher, Academic Press Orlando, FL
    • G. Johansson Partitioning in Aqueous Two-phase Systems H. Walter, D.E. Brooks, D. Fisher, 1986 Academic Press Orlando, FL 161 266
    • (1986) Partitioning in Aqueous Two-phase Systems , pp. 161-266
    • Johansson, G.1
  • 82
    • 84859780593 scopus 로고    scopus 로고
    • Equilibrium phase behavior of poly(ethylene glycol) 4000 and biodegradable salts at various temperatures [(20, 30, and 40) C]
    • R. Duraiayya, S. Arumugam, and S. Settu Equilibrium phase behavior of poly(ethylene glycol) 4000 and biodegradable salts at various temperatures [(20, 30, and 40) C] J. Chem. Eng. Data 57 2012 1112 1117
    • (2012) J. Chem. Eng. Data , vol.57 , pp. 1112-1117
    • Duraiayya, R.1    Arumugam, S.2    Settu, S.3
  • 84
  • 85
    • 0035865710 scopus 로고    scopus 로고
    • Comparison between the thermodynamic features of alpha1-antitrypsin and human albumin partitioning in aqueous two-phase systems of polyethyleneglycol- dextran
    • H. Di Nucci, B. Nerli, and G. Pico Comparison between the thermodynamic features of alpha1-antitrypsin and human albumin partitioning in aqueous two-phase systems of polyethyleneglycol-dextran Biophys. Chem. 89 2001 219 229
    • (2001) Biophys. Chem. , vol.89 , pp. 219-229
    • Di Nucci, H.1    Nerli, B.2    Pico, G.3
  • 86
    • 0035946262 scopus 로고    scopus 로고
    • Purification of recombinant HBc antigen expressed in Escherichia coli and Pichia pastoris: Comparison of size-exclusion chromatography and ultracentrifugation
    • D. Rolland, M. Gauthier, J.M. Dugua, C. Fournier, L. Delpech, B. Watelet, O. Letourneur, M. Arnaud, and M. Jolivet Purification of recombinant HBc antigen expressed in Escherichia coli and Pichia pastoris: comparison of size-exclusion chromatography and ultracentrifugation J. Chromatogr. B 753 2001 51 65
    • (2001) J. Chromatogr. B , vol.753 , pp. 51-65
    • Rolland, D.1    Gauthier, M.2    Dugua, J.M.3    Fournier, C.4    Delpech, L.5    Watelet, B.6    Letourneur, O.7    Arnaud, M.8    Jolivet, M.9
  • 87
    • 67649344468 scopus 로고    scopus 로고
    • A preparative purification process for recombinant hepatitis B core antigen using online capture by expanded bed adsorption followed by size-exclusion chromatography
    • C.W. Ho, W.S. Tan, F.C. Chong, T.C. Ling, and B.T. Tey A preparative purification process for recombinant hepatitis B core antigen using online capture by expanded bed adsorption followed by size-exclusion chromatography J. Microbiol. Biotechnol. 19 2009 416 423
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 416-423
    • Ho, C.W.1    Tan, W.S.2    Chong, F.C.3    Ling, T.C.4    Tey, B.T.5
  • 88
    • 0028928193 scopus 로고
    • Selection of peptide inhibitors of interactions involved in complex protein assemblies: Association of the core and surface antigens of hepatitis B virus
    • M.R. Dyson, and K. Murray Selection of peptide inhibitors of interactions involved in complex protein assemblies: association of the core and surface antigens of hepatitis B virus Proc. Natl. Acad. Sci. USA 92 1995 2194 2198
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2194-2198
    • Dyson, M.R.1    Murray, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.