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Volumn 1, Issue 3, 2006, Pages 1213-1222

Expanded-bed adsorption immobilized-metal affinity chromatography

Author keywords

[No Author keywords available]

Indexed keywords

HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; METAL; OLIGOPEPTIDE; PROTEIN; UNCLASSIFIED DRUG;

EID: 33845568399     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.127     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 17144417370 scopus 로고    scopus 로고
    • Biochemical engineering aspects of expanded bed adsorption
    • Hubbuch, J., Thommes, J. & Kula, M.R. Biochemical engineering aspects of expanded bed adsorption. Adv. Biochem. Eng. Biotechnol. 92, 101-123 (2005).
    • (2005) Adv. Biochem. Eng. Biotechnol , vol.92 , pp. 101-123
    • Hubbuch, J.1    Thommes, J.2    Kula, M.R.3
  • 2
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • Jahic, M., Gustavsson, M., Jansen, A.K., Martinelle, M. & Enfors, S.O. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J Biotechnol. 102, 45-53 (2003).
    • (2003) J Biotechnol , vol.102 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.O.5
  • 3
    • 12144251696 scopus 로고    scopus 로고
    • Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: Case study with recombinant ovine interferon-τ
    • Sinha, J., Plantz, B.A., Inan, M. & Meagher, M.M. Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: Case study with recombinant ovine interferon-τ. Biotechnol. Bioeng. 89, 102-112 (2005).
    • (2005) Biotechnol. Bioeng , vol.89 , pp. 102-112
    • Sinha, J.1    Plantz, B.A.2    Inan, M.3    Meagher, M.M.4
  • 4
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick, S., Fazenda, M.L., McNeil, B. & Harvey, L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 22, 249-270 (2005).
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 5
    • 33845593592 scopus 로고    scopus 로고
    • Production of recombinant protein in Pichia pastoris by fermentation
    • Tolner, B., Smith, L., Begent, R.H.J. & Chester, K.A. Production of recombinant protein in Pichia pastoris by fermentation. Nat. Protocols 1, 1006-1021 (2006).
    • (2006) Nat. Protocols , vol.1 , pp. 1006-1021
    • Tolner, B.1    Smith, L.2    Begent, R.H.J.3    Chester, K.A.4
  • 6
    • 13944266719 scopus 로고    scopus 로고
    • Quantitative immuno-positron emission tomography imaging of HER2-positive tumor xenografts with an iodine-124 labeled anti-HER2 diabody
    • Robinson, M.K. et al. Quantitative immuno-positron emission tomography imaging of HER2-positive tumor xenografts with an iodine-124 labeled anti-HER2 diabody. Cancer Res. 65, 1471-1478 (2005).
    • (2005) Cancer Res , vol.65 , pp. 1471-1478
    • Robinson, M.K.1
  • 7
    • 19944427731 scopus 로고    scopus 로고
    • Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy
    • Sharma, S.K. et al. Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy. Clin. Cancer Res. 11 814-825 (2005).
    • (2005) Clin. Cancer Res , vol.11 , pp. 814-825
    • Sharma, S.K.1
  • 8
    • 3042784498 scopus 로고    scopus 로고
    • Modifying an immunogenic epitope on a therapeutic protein: A step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT)
    • Mayer, A. et al. Modifying an immunogenic epitope on a therapeutic protein: A step towards an improved system for antibody-directed enzyme prodrug therapy (ADEPT). Br. J. Cancer 90, 2402-2410 (2004).
    • (2004) Br. J. Cancer , vol.90 , pp. 2402-2410
    • Mayer, A.1
  • 9
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar, V. & Menart, V. Perspectives of immobilized-metal affinity chromatography. J. Biochem. Biophys. Methods 49, 335-360 (2001).
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 10
    • 32644473166 scopus 로고    scopus 로고
    • Recovery of recombinant β-glucosidase by expanded bed adsorption from Pichia pastoris high-cell-density culture broth
    • Charoenrat, T., Ketudat-Cairns, M., Jahic, M., Enfors, S.O. & Veide, A. Recovery of recombinant β-glucosidase by expanded bed adsorption from Pichia pastoris high-cell-density culture broth. J. Biotechnol. 122, 86-98 (2006).
    • (2006) J. Biotechnol , vol.122 , pp. 86-98
    • Charoenrat, T.1    Ketudat-Cairns, M.2    Jahic, M.3    Enfors, S.O.4    Veide, A.5
  • 12
    • 13844266559 scopus 로고    scopus 로고
    • Single step purification of a series of wheat recombinant proteins with expanded bed absorption chromatography
    • de Lamotte, F. Single step purification of a series of wheat recombinant proteins with expanded bed absorption chromatography. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 818, 29-33 (2005).
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.818 , pp. 29-33
    • de Lamotte, F.1
  • 13
    • 33646014160 scopus 로고    scopus 로고
    • Purification of recombinant histidine-tag streptolysin O using immobilized metal affinity expanded bed adsorption (IMA-EBA)
    • Camprubi, S., Bruguera, M. & Canalias, F. Purification of recombinant histidine-tag streptolysin O using immobilized metal affinity expanded bed adsorption (IMA-EBA). Int. J. Biol. Macromol. 38, 134-139 (2006).
    • (2006) Int. J. Biol. Macromol , vol.38 , pp. 134-139
    • Camprubi, S.1    Bruguera, M.2    Canalias, F.3
  • 14
    • 13844255323 scopus 로고    scopus 로고
    • LdARL-1 His-tagged recombinant protein: Purification by immobilized metal affinity expanded bed adsorption
    • Sahin, A., Tetaud, E., Merlin, G. & Santarelli, X. LdARL-1 His-tagged recombinant protein: Purification by immobilized metal affinity expanded bed adsorption. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 818, 19-22 (2005).
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.818 , pp. 19-22
    • Sahin, A.1    Tetaud, E.2    Merlin, G.3    Santarelli, X.4
  • 15
    • 0036862029 scopus 로고    scopus 로고
    • On-line purification of monoclonal antibodies using an integrated stirred-tank reactor/expanded-bed adsorption system
    • Ohashi, R., Otero, J.M., Chwistek, A., Yamato, I. & Hamel, J.F. On-line purification of monoclonal antibodies using an integrated stirred-tank reactor/expanded-bed adsorption system. Biotechnol. Prog. 28 1292-1300 (2002).
    • (2002) Biotechnol. Prog , vol.28 , pp. 1292-1300
    • Ohashi, R.1    Otero, J.M.2    Chwistek, A.3    Yamato, I.4    Hamel, J.F.5
  • 16
    • 0041347563 scopus 로고    scopus 로고
    • Large-scale purification of an antibody directed against hepatitis B surface antigen from transgenic tobacco plants
    • Valdes, R. et al. Large-scale purification of an antibody directed against hepatitis B surface antigen from transgenic tobacco plants. Biochem. Biophys. Res. Commun. 308, 94-100 (2003).
    • (2003) Biochem. Biophys. Res. Commun , vol.308 , pp. 94-100
    • Valdes, R.1
  • 17
    • 30944433166 scopus 로고    scopus 로고
    • Expanded bed adsorption as a primary recovery step for the isolation of the insulin precursor MI3 process development and scale up
    • Brixius, P. et al. Expanded bed adsorption as a primary recovery step for the isolation of the insulin precursor MI3 process development and scale up. Biotechnol. Bioeng. 93, 14-20 (2006).
    • (2006) Biotechnol. Bioeng , vol.93 , pp. 14-20
    • Brixius, P.1
  • 18
    • 33747760712 scopus 로고    scopus 로고
    • Method for large-scale isolation and purification of R-phycoerythrin from red alga Polysiphonia urceolata Grev
    • Niu, J.F., Wang, G.C. & Tseng, C.K. Method for large-scale isolation and purification of R-phycoerythrin from red alga Polysiphonia urceolata Grev. Protein Expr. Purif. 49, 23-31 (2006).
    • (2006) Protein Expr. Purif , vol.49 , pp. 23-31
    • Niu, J.F.1    Wang, G.C.2    Tseng, C.K.3
  • 20
    • 33645465485 scopus 로고    scopus 로고
    • Expanded bed adsorption as a fast technique for the large-scale purification of the complete isoform pool of Ber e 1, the major allergen from Brazil nuts
    • Van Boxtel, E.L. et al. Expanded bed adsorption as a fast technique for the large-scale purification of the complete isoform pool of Ber e 1, the major allergen from Brazil nuts. Mol. Nutr. Food Res. 50, 275-281 (2006).
    • (2006) Mol. Nutr. Food Res , vol.50 , pp. 275-281
    • Van Boxtel, E.L.1
  • 21
    • 13844297856 scopus 로고    scopus 로고
    • Purification and on-column refolding of EGFP overexpressed as inclusion bodies in Escherichia coli with expanded bed anion exchange chromatography
    • Cabanne, C. et al. Purification and on-column refolding of EGFP overexpressed as inclusion bodies in Escherichia coli with expanded bed anion exchange chromatography, J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 818, 23-27 (2005).
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.818 , pp. 23-27
    • Cabanne, C.1
  • 22
    • 33644918876 scopus 로고    scopus 로고
    • On-column refolding of recombinant human interferon-γ inclusion bodies by expanded bed adsorption chromatography
    • Jin, T., Guan, Y.X., Yao, S.J., Lin, D.Q. & Cho, M.G. On-column refolding of recombinant human interferon-γ inclusion bodies by expanded bed adsorption chromatography. Biotechnol. Bioeng. 93 755-760 (2006).
    • (2006) Biotechnol. Bioeng , vol.93 , pp. 755-760
    • Jin, T.1    Guan, Y.X.2    Yao, S.J.3    Lin, D.Q.4    Cho, M.G.5
  • 23
    • 0028836167 scopus 로고
    • Purification of bacterially expressed single chain Fv antibodies for clinical applications using metal chelate chromatography
    • Casey, J.L. et al. Purification of bacterially expressed single chain Fv antibodies for clinical applications using metal chelate chromatography. J. Immunol. Methods 179, 105-116 (1995).
    • (1995) J. Immunol. Methods , vol.179 , pp. 105-116
    • Casey, J.L.1
  • 24
    • 0029294084 scopus 로고
    • In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library
    • Schier, R. et al. In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library. Immunotechnology 1, 73-81 (1995).
    • (1995) Immunotechnology , vol.1 , pp. 73-81
    • Schier, R.1
  • 25
    • 4143129879 scopus 로고    scopus 로고
    • Directed evolution of an anti-carcinoembryonic antigen scFv with a 4-day monovalent dissociation half-time at 37 °C
    • Graff, C.P., Chester, K., Begent, R. & Wittrup, K.D. Directed evolution of an anti-carcinoembryonic antigen scFv with a 4-day monovalent dissociation half-time at 37 °C. Protein Eng. Des. Sel. 17, 293-304 (2004).
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 293-304
    • Graff, C.P.1    Chester, K.2    Begent, R.3    Wittrup, K.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.