메뉴 건너뛰기




Volumn 84, Issue 1 C, 2006, Pages 28-36

Utilization of group specific ligands in the downstream processing of proteins by affinity precipitation

Author keywords

Affinity chromatography; His tag; IMAC; LCST; PolyNIPAAm; Protein A; Stimuli responsive materials

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHEMICAL BONDS; MOLECULES; PRECIPITATION (CHEMICAL); SOLUBILITY;

EID: 33646591880     PISSN: 09603085     EISSN: None     Source Type: Journal    
DOI: 10.1205/fbp.05153     Document Type: Article
Times cited : (12)

References (48)
  • 1
    • 0032632898 scopus 로고    scopus 로고
    • Investigation of the LCST of polyacrylamides as a function of molecular parameters and solvent composition
    • Baltes, T., Garret-Flaudy, F. and Freitag, R., 1999, Investigation of the LCST of polyacrylamides as a function of molecular parameters and solvent composition, J Polym Sci A, Polym Chem, 37: 2977-2989.
    • (1999) J Polym Sci A, Polym Chem , vol.37 , pp. 2977-2989
    • Baltes, T.1    Garret-Flaudy, F.2    Freitag, R.3
  • 2
    • 0036317353 scopus 로고    scopus 로고
    • Therapeutic applications of monoclonal antibodies
    • Berger, M., Shankar, V. and Vafai, A., 2002, Therapeutic applications of monoclonal antibodies, Am J Med Sci, 324: 14-30.
    • (2002) Am J Med Sci , vol.324 , pp. 14-30
    • Berger, M.1    Shankar, V.2    Vafai, A.3
  • 3
    • 0035975882 scopus 로고    scopus 로고
    • Twenty-five years of immobilized metal ion affinity chromatography: Past, present and future
    • Chaga, G.S., 2001, Twenty-five years of immobilized metal ion affinity chromatography: past, present and future, J Biochem Biophys Methods, 49(1-3): 313-334.
    • (2001) J Biochem Biophys Methods , vol.49 , Issue.1-3 , pp. 313-334
    • Chaga, G.S.1
  • 4
    • 0027329784 scopus 로고
    • Preparation and properties of thermo-Reversible, phase-separating enzyme-oligo(N-isopropylacrylamide) conjugates
    • Chen, G. and Hoffman, A.S., 1993, Preparation and properties of thermo-reversible, phase-separating enzyme-oligo(N-isopropylacrylamide) conjugates, Bioconjugate Chem, 4: 509-514.
    • (1993) Bioconjugate Chem , vol.4 , pp. 509-514
    • Chen, G.1    Hoffman, A.S.2
  • 5
    • 0025646474 scopus 로고
    • Polymer-protein conjugates: II. Affinity precipitation separation of human immunogammaglobulin by a poly(N-isopropylacrylamide)-protein A conjugate
    • Chen, J.P. and Hoffman, A.S., 1990, Polymer-protein conjugates: II. Affinity precipitation separation of human immunogammaglobulin by a poly(N-isopropylacrylamide)-protein A conjugate, Biomaterials, 11: 631-634.
    • (1990) Biomaterials , vol.11 , pp. 631-634
    • Chen, J.P.1    Hoffman, A.S.2
  • 6
    • 0037420336 scopus 로고    scopus 로고
    • DNA purification by triple helix affinity precipitation: The THAP process
    • Costioli, M., Fisch, I., Garret-Flaudy, F., Hilbrig, F. and Freitag R., 2003, DNA purification by triple helix affinity precipitation: The THAP process. Biotechnol Bioeng, 81(5): 535-545.
    • (2003) Biotechnol Bioeng , vol.81 , Issue.5 , pp. 535-545
    • Costioli, M.1    Fisch, I.2    Garret-Flaudy, F.3    Hilbrig, F.4    Freitag, R.5
  • 7
    • 0032313523 scopus 로고    scopus 로고
    • Affinity precipitation of monoclonal antibodies by nonstoichiometric polyelectrolyte complexes
    • Dainiak, M.B., Izumrudov, V.A., Muronetz, V.I., Galaev, I.Y. and Mattiasson, B., 1998, Affinity precipitation of monoclonal antibodies by nonstoichiometric polyelectrolyte complexes, Bioseparation, 7: 231-240.
    • (1998) Bioseparation , vol.7 , pp. 231-240
    • Dainiak, M.B.1    Izumrudov, V.A.2    Muronetz, V.I.3    Galaev, I.Y.4    Mattiasson, B.5
  • 8
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution
    • Deisenhofer, J., 1981, Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution, Biochemistry, 20: 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 9
    • 0033199280 scopus 로고    scopus 로고
    • Thermoprecipitation of streptavidin via oligonucleotide-mediated self-assembly with poly(N-isopropylacrylamide)
    • Fong, R.B., Ding, Z., Long, C.J., Hoffman, A.S. and Stayton, P.S., 1999, Thermoprecipitation of streptavidin via oligonucleotide-mediated self-assembly with poly(N-isopropylacrylamide), Bioconjugate Chemistry, 10: 720-725.
    • (1999) Bioconjugate Chemistry , vol.10 , pp. 720-725
    • Fong, R.B.1    Ding, Z.2    Long, C.J.3    Hoffman, A.S.4    Stayton, P.S.5
  • 10
    • 0037026239 scopus 로고    scopus 로고
    • Affinity separation using an Fv antibody fragment-smart polymer conjugate
    • Fong, R.B., Ding, Z., Hoffman, A.S. and Stayton, P.S., 2002, Affinity separation using an Fv antibody fragment-smart polymer conjugate, Biotechnol Bioeng, 79: 271-276.
    • (2002) Biotechnol Bioeng , vol.79 , pp. 271-276
    • Fong, R.B.1    Ding, Z.2    Hoffman, A.S.3    Stayton, P.S.4
  • 11
    • 0013992053 scopus 로고
    • 'Protein A' from S. aureus: I. Pseudo-immune reaction with human immunoglobulin
    • Forsgren, A. and Sjoquist, J., 1966, 'Protein A' from S. aureus: I. Pseudo-immune reaction with human immunoglobulin, J Immunol, 97: 822-827.
    • (1966) J Immunol , vol.97 , pp. 822-827
    • Forsgren, A.1    Sjoquist, J.2
  • 12
    • 33646576696 scopus 로고    scopus 로고
    • Affinity precipitation: Stimulus-responsive polymers for bioseparation
    • Freitag, R. (ed.). (Landes Biosciences, Biotechnology Intelligence Unit 4, Landes Biosciences, Eurekah-Com, Austin, Tx, USA)
    • Freitag, R., 2003, Affinity precipitation: Stimulus-responsive polymers for bioseparation, in Freitag, R. (ed.). Synthetic Polymers in Biotechnology and Medicine. (Landes Biosciences, Biotechnology Intelligence Unit 4, Landes Biosciences, Eurekah-Com, Austin, Tx, USA).
    • (2003) Synthetic Polymers in Biotechnology and Medicine
    • Freitag, R.1
  • 13
    • 33646592998 scopus 로고    scopus 로고
    • Affinity macroligands
    • US 6,258,275 BIR
    • Freitag, R. and Garret-Flandy, F., 2001, Affinity macroligands, US 6,258,275 BIR.
    • (2001)
    • Freitag, R.1    Garret-Flandy, F.2
  • 14
    • 0037198243 scopus 로고    scopus 로고
    • Salt effects on the thermo-precipitation of poly-(N-isopropylacrylamide) from aqueous solution
    • Freitag, R. and Garret-Flandy, F., 2002, Salt effects on the thermo-precipitation of poly-(N-isopropylacrylamide) from aqueous solution, Langmuir, 18(9): 3434-3440.
    • (2002) Langmuir , vol.18 , Issue.9 , pp. 3434-3440
    • Freitag, R.1    Garret-Flandy, F.2
  • 15
    • 85030609234 scopus 로고    scopus 로고
    • Use of the Avidin (Imino)biotin system as a general approach to affinity precipitation
    • (The Humana Press Inc., Totowa, New Jersey, USA)
    • Freitag, R. and Hilbrig, F., 2005, Use of the Avidin (Imino)biotin system as a general approach to affinity precipitation, Methods in Molecular Biology Book Series (The Humana Press Inc., Totowa, New Jersey, USA).
    • (2005) Methods in Molecular Biology Book Series
    • Freitag, R.1    Hilbrig, F.2
  • 16
    • 0027592277 scopus 로고
    • Thermoreactive, water-soluble polymers, non-ionic surfactants, and hydrogels as reagents in biotechnology
    • Galaev, I.Y. and Mattiasson, B., 1993, Thermoreactive, water-soluble polymers, non-ionic surfactants, and hydrogels as reagents in biotechnology, Enzyme Microb Technol, 15: 354-366.
    • (1993) Enzyme Microb Technol , vol.15 , pp. 354-366
    • Galaev, I.Y.1    Mattiasson, B.2
  • 17
    • 0033178588 scopus 로고    scopus 로고
    • 'Smart' polymers and what they could do in biotechnology and medicine
    • Galaev, I.Y. and Mattiasson, B., 1999, 'Smart' polymers and what they could do in biotechnology and medicine, TIBTECH, 17: 335-340.
    • (1999) TIBTECH , vol.17 , pp. 335-340
    • Galaev, I.Y.1    Mattiasson, B.2
  • 18
    • 0034449308 scopus 로고    scopus 로고
    • Use of the avidin (imino)biotin system as a general approach to affinity precipitation
    • Garret-Flaudy, F. and Freitag, R., 2001, Use of the avidin (imino)biotin system as a general approach to affinity precipitation, Biotechnol Bioeng, 71: 223-234.
    • (2001) Biotechnol Bioeng , vol.71 , pp. 223-234
    • Garret-Flaudy, F.1    Freitag, R.2
  • 19
    • 0030183068 scopus 로고    scopus 로고
    • Dye-aftinity techniques for bioprocessing: Recent developments
    • Garg, N., Galaev, I.Y. and Mattiasson, B., 1996, Dye-aftinity techniques for bioprocessing: Recent developments, J Mol Recog, 9(4): 259-274.
    • (1996) J Mol Recog , vol.9 , Issue.4 , pp. 259-274
    • Garg, N.1    Galaev, I.Y.2    Mattiasson, B.3
  • 20
    • 0028431520 scopus 로고
    • Monoclonal antibody purification guide: Part 1-3
    • (7): 12-14, (8): 16-18
    • Grandics, P., 1994, Monoclonal antibody purification guide: Part 1-3. Am Biotechnol Lab, 12(6): 58-62, (7): 12-14, (8): 16-18.
    • (1994) Am Biotechnol Lab , vol.12 , Issue.6 , pp. 58-62
    • Grandics, P.1
  • 21
    • 77956990599 scopus 로고
    • Spectrophotometric determination of avidin and biotin
    • Green, N.M., 1970, Spectrophotometric determination of avidin and biotin, Meth Enzymol, 18A: 418-424.
    • (1970) Meth Enzymol , vol.18 A , pp. 418-424
    • Green, N.M.1
  • 23
    • 0038739516 scopus 로고    scopus 로고
    • Protein purification by affinity precipitation
    • Hilbrig, F. and Freitag, R., 2003, Protein purification by affinity precipitation, J Chromatogr B, 790: 79-90.
    • (2003) J Chromatogr B , vol.790 , pp. 79-90
    • Hilbrig, F.1    Freitag, R.2
  • 25
    • 20344386976 scopus 로고    scopus 로고
    • Temperature-triggered purification of antibodies
    • Kim, J.-Y., Mulchandani, A. and Chen, W., 2005, Temperature-triggered purification of antibodies, Biotechnol Bioeng, 90: 373-379.
    • (2005) Biotechnol Bioeng , vol.90 , pp. 373-379
    • Kim, J.-Y.1    Mulchandani, A.2    Chen, W.3
  • 26
    • 0028765276 scopus 로고
    • Development and application of thermosensitve immunomicrospheres for antibody purification
    • Kondo, A., Kanejko, T. and Higashitani, K., 1994, Development and application of thermosensitve immunomicrospheres for antibody purification, Biotechnol Bioeng, 44: 1-6.
    • (1994) Biotechnol Bioeng , vol.44 , pp. 1-6
    • Kondo, A.1    Kanejko, T.2    Higashitani, K.3
  • 27
    • 0015546673 scopus 로고
    • Biological tolerance of poly(N-substituted acrylamides)
    • Kopecek, J., Sprincl, L., Bazilova, H. and Vacik J., 1973, Biological tolerance of poly(N-substituted acrylamides), J Biomed Mater Res, 7: 111-121.
    • (1973) J Biomed Mater Res , vol.7 , pp. 111-121
    • Kopecek, J.1    Sprincl, L.2    Bazilova, H.3    Vacik, J.4
  • 28
    • 0032552491 scopus 로고    scopus 로고
    • Affinity precipitation of α-amylase inhibitor from wheat meal by metal chelate affinity binding using cu(II)-loaded copolymers of 1-vinylimidazole with N-isopropylacrylamide
    • Kumar, A., Galaev, I.Y. and Mattiasson, B., 1998, Affinity precipitation of α-amylase inhibitor from wheat meal by metal chelate affinity binding using cu(II)-loaded copolymers of 1-vinylimidazole with N-isopropylacrylamide, Biotechnol Bioeng, 59: 695-704.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 695-704
    • Kumar, A.1    Galaev, I.Y.2    Mattiasson, B.3
  • 29
    • 0142104893 scopus 로고    scopus 로고
    • Purification of histidine-tagged single-chain Fv-antibody fragments by metal chelate aftinity precipitation using thermoresponsive copolymers
    • Kumar, A., Wahlund, P.-O., Kepka, C., Galaev, I.Y. and Mattiasson, B., 2003, Purification of histidine-tagged single-chain Fv-antibody fragments by metal chelate aftinity precipitation using thermoresponsive copolymers, Biotechnol Bioeng, 84: 494-503.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 494-503
    • Kumar, A.1    Wahlund, P.-O.2    Kepka, C.3    Galaev, I.Y.4    Mattiasson, B.5
  • 30
    • 0028501408 scopus 로고
    • Affinity precipitation of trypsin with soybean trypsin-inhibitor linked eudragit S-100
    • Kumar, A. and Gupta, M.N., 1994, Affinity precipitation of trypsin with soybean trypsin-inhibitor linked eudragit S-100, J Biotechnol, 37: 185-189.
    • (1994) J Biotechnol , vol.37 , pp. 185-189
    • Kumar, A.1    Gupta, M.N.2
  • 31
    • 0030203635 scopus 로고    scopus 로고
    • An assessment of nonspecific adsorption to Eudragit S-100 during affinity precipitation
    • Kumar, A. and Gupta, M.N., 1996, An assessment of nonspecific adsorption to Eudragit S-100 during affinity precipitation, Mol Biotechnol, 6: 1-6.
    • (1996) Mol Biotechnol , vol.6 , pp. 1-6
    • Kumar, A.1    Gupta, M.N.2
  • 32
    • 0020448397 scopus 로고
    • Applications of immobilized protein A in immunochemical techniques
    • Langone, J.J., 1982a, Applications of immobilized protein A in immunochemical techniques, J Immunol Methods, 55: 277-296.
    • (1982) J Immunol Methods , vol.55 , pp. 277-296
    • Langone, J.J.1
  • 33
    • 0020011459 scopus 로고
    • Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci
    • Langone, J.J., 1982b, Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci, Adv Immunol, 32: 157-252.
    • (1982) Adv Immunol , vol.32 , pp. 157-252
    • Langone, J.J.1
  • 34
    • 0030265252 scopus 로고    scopus 로고
    • Affinity precipitation of Concanavalin A with p-aminophenyl-alpha-D-glucopyranoside modified Eudragit S-1002. Kinetic studies of the formation and the dissociation of the protein-macroligand complex
    • Larsson, E.L., Galaev, I.Y. and Mattiasson, B., 1996, Affinity precipitation of Concanavalin A with p-aminophenyl-alpha-D-glucopyranoside modified Eudragit S-1002. Kinetic studies of the formation and the dissociation of the protein-macroligand complex, Bioseparation, 6: 283-291.
    • (1996) Bioseparation , vol.6 , pp. 283-291
    • Larsson, E.L.1    Galaev, I.Y.2    Mattiasson, B.3
  • 35
    • 0025782267 scopus 로고
    • Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails
    • Lilius, G., Persson, M., Bülow, L. and Mosbach, K., 1991, Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails, Eur J Biochem, 198: 499-504.
    • (1991) Eur J Biochem , vol.198 , pp. 499-504
    • Lilius, G.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 36
    • 0024278495 scopus 로고
    • Synthesis and characterization of a water-soluble affinity polymer for trypsin purification
    • Luong, J.H.T., Male, K.B. and Nguyen, A.L., 1988, Synthesis and characterization of a water-soluble affinity polymer for trypsin purification, Biotechnol Bioeng, 31: 439-446.
    • (1988) Biotechnol Bioeng , vol.31 , pp. 439-446
    • Luong, J.H.T.1    Male, K.B.2    Nguyen, A.L.3
  • 37
    • 0032457503 scopus 로고    scopus 로고
    • Affinity precipitation of proteins: Design criteria for an efficient polymer
    • Mattiasson, B., Kumar, A. and Galaev, I.Y., 1998, Affinity precipitation of proteins: design criteria for an efficient polymer, J Mol Recog, 11: 211-216.
    • (1998) J Mol Recog , vol.11 , pp. 211-216
    • Mattiasson, B.1    Kumar, A.2    Galaev, I.Y.3
  • 38
    • 0020211335 scopus 로고
    • A spectrophotometric assay for soluble and immobilized N-hydroxysuccinimide esters
    • Miron, T. and Wilchek, M., 1982, A spectrophotometric assay for soluble and immobilized N-hydroxysuccinimide esters, Anal Biochem, 126: 433-435.
    • (1982) Anal Biochem , vol.126 , pp. 433-435
    • Miron, T.1    Wilchek, M.2
  • 39
    • 0035809089 scopus 로고    scopus 로고
    • Sequence-specific affinity precipitation of oligonucleotide using poly(N-isopropylacrylamide)-Oligonucleotide conjugate
    • Mori, T., Umeno, D. and Maeda, M., 2001, Sequence-specific affinity precipitation of oligonucleotide using poly(N-isopropylacrylamide)-oligonucleotide conjugate, Biotechnol Bioeng, 72: 261-268.
    • (2001) Biotechnol Bioeng , vol.72 , pp. 261-268
    • Mori, T.1    Umeno, D.2    Maeda, M.3
  • 40
    • 0025953368 scopus 로고
    • Affinity precipitation of extracellular microbial enzymes
    • Pecs, M., Eggert, M. and Schügerl, K., 1991, Affinity precipitation of extracellular microbial enzymes, J Biotechnol, 21: 137-142.
    • (1991) J Biotechnol , vol.21 , pp. 137-142
    • Pecs, M.1    Eggert, M.2    Schügerl, K.3
  • 41
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath, J., Carlsson, J., Olsson, J. and Belfrage, G., 1975, Metal chelate affinity chromatography, a new approach to protein fractionation, Nature, 258: 598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, J.3    Belfrage, G.4
  • 42
    • 0004991063 scopus 로고
    • Poly(N-isopropylacrylamide) experiment, theory and application
    • Schild, H.G., 1992, Poly(N-isopropylacrylamide) experiment, theory and application, Prog Polym Sci, 17: 163-249.
    • (1992) Prog Polym Sci , vol.17 , pp. 163-249
    • Schild, H.G.1
  • 43
    • 4243656934 scopus 로고
    • Microcalorimetric detection of lower critical solution temperatures in aqueous polymer solutions
    • Schild, H.G. and Tirrell, D.A., 1990, Microcalorimetric detection of lower critical solution temperatures in aqueous polymer solutions, J Phys Chem, 94: 4352-4356.
    • (1990) J Phys Chem , vol.94 , pp. 4352-4356
    • Schild, H.G.1    Tirrell, D.A.2
  • 44
    • 0027653903 scopus 로고
    • Temperature-responsive bioconjugates. 2. Molecular design for temperature-modulated bioseparation
    • Takei, Y.G., Aoki, T., Sanui, K., Ogata, N., Okano, T. and Sakurai, Y., 1993, Temperature-responsive bioconjugates. 2. Molecular design for temperature-modulated bioseparation, Bioconjugate Chem, 4: 341-346.
    • (1993) Bioconjugate Chem , vol.4 , pp. 341-346
    • Takei, Y.G.1    Aoki, T.2    Sanui, K.3    Ogata, N.4    Okano, T.5    Sakurai, Y.6
  • 45
    • 0028539339 scopus 로고
    • Temperature-responsive bioconjugates. 3. Antibody-poly(N-isopropylacrylamide) conjugates for temperature-modulated
    • Takei, Y.G., Matsukata, M., Aoki, T., Sanui, K., Ogata, N., Kikuchi, A., Sakurai, Y. and Okano, T., 1994, Temperature-responsive bioconjugates. 3. Antibody-poly(N-isopropylacrylamide) conjugates for temperature-modulated precipitations and affinity bioseparations, Bioconjugate Chem, 6: 577-582. precipitations and affinity bioseparations
    • (1994) Bioconjugate Chem , vol.6 , pp. 577-582
    • Takei, Y.G.1    Matsukata, M.2    Aoki, T.3    Sanui, K.4    Ogata, N.5    Kikuchi, A.6    Sakurai, Y.7    Okano, T.8
  • 46
    • 0032213085 scopus 로고    scopus 로고
    • Water-soluble conjugate of double-stranded dna and poly(N-isopropylacrylamide) for one-pot affinity precipitation separation of DNA-binding proteins
    • Umeno, D., Kawasaki, M. and Maeda, M., 1998, Water-soluble conjugate of double-stranded dna and poly(N-isopropylacrylamide) for one-pot affinity precipitation separation of DNA-binding proteins, Bioconjugate Chem, 9: 719-724.
    • (1998) Bioconjugate Chem , vol.9 , pp. 719-724
    • Umeno, D.1    Kawasaki, M.2    Maeda, M.3
  • 48
    • 33646587516 scopus 로고    scopus 로고
    • Purification of antibodies by chromatographic methods
    • Subramanian, S. (ed.). (Kluwer Academic/Plenum Publishers)
    • Vandevyver, C. and Freitag, R., 2003, Purification of antibodies by chromatographic methods, in Subramanian, S. (ed.). Biopharmaceutical Antibodies: Production, Purification and Safety, Vol 1, (Kluwer Academic/ Plenum Publishers).
    • (2003) Biopharmaceutical Antibodies: Production, Purification and Safety , vol.1
    • Vandevyver, C.1    Freitag, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.