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Volumn 5, Issue 5, 2010, Pages 477-483

Interaction mechanism of mono-PEGylated proteins in electrostatic interaction chromatography

Author keywords

Binding site; Biochemical engineering; Electrostatic interaction; Ion exchange chromatography; PEGylation

Indexed keywords

BINDING MECHANISMS; BOVINE SERUM ALBUMINS; COVALENT ATTACHMENT; DEVELOPED MODEL; ELECTROSTATIC INTERACTION CHROMATOGRAPHY; ELECTROSTATIC INTERACTIONS; ELUTION VOLUMES; INTERACTION MECHANISMS; ION-EXCHANGE CHROMATOGRAPHY; MODEL PROTEINS; PEGYLATED PROTEINS; PEGYLATION; PROTEIN RETENTION; SMALL MOLECULES; STERIC HINDRANCES;

EID: 77952154264     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201000013     Document Type: Article
Times cited : (37)

References (28)
  • 1
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski, A., Van Es, T., Palczuk, N. C., Davis, F. F., Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem. 1977, 252, 3578-3581.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    Van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 5
    • 27844515221 scopus 로고    scopus 로고
    • PEG-proteins: Reaction engineering and separation issues
    • Fee, C. J., Van Alstine, J. M., PEG-proteins: Reaction engineering and separation issues. Chem. Eng. Sci. 2006, 61, 934-939.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 934-939
    • Fee, C.J.1    Van Alstine, J.M.2
  • 6
    • 0035951339 scopus 로고    scopus 로고
    • Use of ion-exchange chromatography and hydrophobic interaction chromatography in the preparation and recovery of polyethylene glycol-linked proteins
    • Seely, J. E., Richey, C.W., Use of ion-exchange chromatography and hydrophobic interaction chromatography in the preparation and recovery of polyethylene glycol-linked proteins. J. Chromatogr. A 2001, 908, 235-241.
    • (2001) J. Chromatogr. A , vol.908 , pp. 235-241
    • Seely, J.E.1    Richey, C.W.2
  • 7
    • 77952224043 scopus 로고    scopus 로고
    • Protein conjugates purification and characterization
    • Veronese, F.M. (Ed.), Birkhauser, Basel
    • Fee, C. J., Protein conjugates purification and characterization, in Veronese, F.M. (Ed.), PEGylated Protein Drugs: Basic Science and Clinical Applications, Birkhauser, Basel 2009, pp. 113-125.
    • (2009) PEGylated Protein Drugs: Basic Science and Clinical Applications , pp. 113-125
    • Fee, C.J.1
  • 8
    • 0037457502 scopus 로고    scopus 로고
    • Size-exclusions reaction chromatography (SERC): A new technique for protein pegylation
    • Fee, C. J., Size-exclusions reaction chromatography (SERC): A new technique for protein pegylation. Biotechnol. Bioeng. 2003, 82, 200-206.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 200-206
    • Fee, C.J.1
  • 9
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins
    • Fee, C. J., Van Alstine, J. M., Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins. Bioconj. Chem. 2004, 15, 1304-1313.
    • (2004) Bioconj. Chem. , vol.15 , pp. 1304-1313
    • Fee, C.J.1    Van Alstine, J.M.2
  • 11
    • 36849030716 scopus 로고    scopus 로고
    • Overview of the lysozyme-monomethoxypolyethylene glycol conjugate as a model for protein tailoring
    • DOI 10.1295/koron.64.716
    • Nodake, Y., Sakakibara, R., Yamasaki, N., Overview of the lysozyme-monomethoxypolyethylene glycol conjugate as a model for protein tailoring. Kobunshi Ronbunshu 2007. 64, 716-726. (Pubitemid 350218529)
    • (2007) Kobunshi Ronbunshu , vol.64 , Issue.11 , pp. 716-726
    • Nodake, Y.1    Sakakibara, R.2    Yamasaki, N.3
  • 12
    • 33947502313 scopus 로고    scopus 로고
    • Comparison of strong anion-exchangers for the purification of a PEGylated protein
    • Pabst, T. M., Buckley, J. J., Ramasubramanyan, N., Hunter, A. K., Comparison of strong anion-exchangers for the purification of a PEGylated protein. J. Chromatogr. A 2007, 1147, 172-182.
    • (2007) J. Chromatogr. A , vol.1147 , pp. 172-182
    • Pabst, T.M.1    Buckley, J.J.2    Ramasubramanyan, N.3    Hunter, A.K.4
  • 13
    • 35348946448 scopus 로고    scopus 로고
    • Effects of protein conformational changes on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins
    • DOI 10.1016/j.jbiotec.2007.05.028, PII S0168165607003768, Advances in Biochemical Engineering Science
    • Yamamoto, S., Fujii, S., Yoshimoto, N., Akbaruzadehlaleh, P., Effects of protein conformational change on separation performance in electrostatic interaction chromatography: Unfolded proteins and PEGylated proteins. J. Biotechnol. 2007, 132, 196-201. (Pubitemid 47603200)
    • (2007) Journal of Biotechnology , vol.132 , Issue.2 , pp. 196-201
    • Yamamoto, S.1    Fujii, S.2    Yoshimoto, N.3    Akbarzadehlaleh, P.4
  • 14
    • 28144445191 scopus 로고    scopus 로고
    • Electrostatic interaction chromatography process for protein separations: The impact of the engineering analysis of biorecognition mechanism on the process optimization
    • Yamamoto, S., Electrostatic interaction chromatography process for protein separations: The impact of the engineering analysis of biorecognition mechanism on the process optimization. Chem. Eng. Technol. 2005, 28, 1387-1393.
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1387-1393
    • Yamamoto, S.1
  • 16
    • 0035858376 scopus 로고    scopus 로고
    • Pronounced activity of enzymes through the incorporation into the core of polyion complex micelles made from charged block copolymers
    • DOI 10.1016/S0168-3659(01)00264-4, PII S0168365901002644
    • Harada, A., Kataoka, K., Pronounced activity of enzymes through the incorporation into the core of polyion complex micelles made from charged block copolymers. J. Control. Release 2001, 72, 85-91. (Pubitemid 32522346)
    • (2001) Journal of Controlled Release , vol.72 , Issue.1-3 , pp. 85-91
    • Harada, A.1    Kataoka, K.2
  • 17
    • 0022108709 scopus 로고
    • Enhancement of the sensitivity of a fluorometric lysozyme assay system by adding β-N-acetylhexosaminidase
    • Fukuda, H., Tanimoto, T., Yamaha, T., Enhancement of the sensitivity of a fluorometric lysozyme assay system by adding β-N-acetylhexosaminidase. Chem. Pharm. Bull. 1985, 33, 3375-3380.
    • (1985) Chem. Pharm. Bull. , vol.33 , pp. 3375-3380
    • Fukuda, H.1    Tanimoto, T.2    Yamaha, T.3
  • 18
    • 0038010128 scopus 로고    scopus 로고
    • Isolation, structural characterization, and antiviral activity of positional isomers of monopegylated interferon α-2a(PEGASYS)
    • Foser, S., Schacher, A., Weyer, K. A., Brugger, D. et al., Isolation, structural characterization, and antiviral activity of positional isomers of monopegylated interferon α-2a(PEGASYS). Protein Expr. Purif. 2003, 30, 78-87.
    • (2003) Protein Expr. Purif. , vol.30 , pp. 78-87
    • Foser, S.1    Schacher, A.2    Weyer, K.A.3    Brugger, D.4
  • 19
    • 26844510432 scopus 로고    scopus 로고
    • Rational methods for predicting human monoclonal antibodies retention in protein a affinity chromatography and cation exchange chromatography: Structure-based chromatography design for monoclonal antibodies
    • Ishihara, T., Kadoya, T., Yoshida, H., Tamada, T., Yamamoto, S., Rational methods for predicting human monoclonal antibodies retention in protein a affinity chromatography and cation exchange chromatography: Structure-based chromatography design for monoclonal antibodies. J. Chromatogr. A 2005, 1093, 126-138.
    • (2005) J. Chromatogr. A , vol.1093 , pp. 126-138
    • Ishihara, T.1    Kadoya, T.2    Yoshida, H.3    Tamada, T.4    Yamamoto, S.5
  • 20
    • 33847215513 scopus 로고    scopus 로고
    • Retention studies of DNA on anion-exchange monolith chromatography. Binding site and elution behavior
    • DOI 10.1016/j.chroma.2007.01.025, PII S0021967307000714, 2nd Summer School on Monolith Technology for Biochromatography, Bioconversion and Solid-Phase Synthesis
    • Yamamoto, S., Nakamura, M., Tarmann, C., Jungbauer, A., Retention studies of DNA on anion-exchange monolith chromatography: Binding site and elution behavior. J. Chromatogr. A 2007, 1144, 155-160. (Pubitemid 46298854)
    • (2007) Journal of Chromatography a , vol.1144 , Issue.1 , pp. 155-160
    • Yamamoto, S.1    Nakamura, M.2    Tarmann, C.3    Jungbauer, A.4
  • 21
    • 70349829161 scopus 로고    scopus 로고
    • Binding and elution behavior of proteins on strong cation exchangers
    • Pabst, T. M., Suda, E. J., Thomas, K. E., Mensah, P. et al., Binding and elution behavior of proteins on strong cation exchangers. J. Chromatogr. A 2009, 1216, 7950-7956.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7950-7956
    • Pabst, T.M.1    Suda, E.J.2    Thomas, K.E.3    Mensah, P.4
  • 22
    • 66249103015 scopus 로고    scopus 로고
    • Comparison of agarose and dextran-grafted agarose strong ion exchangers for the separation of protein aggregates
    • Suda, E. J., Thomas, K. E., Pabst, T. M., Mensah, P. et al., Comparison of agarose and dextran-grafted agarose strong ion exchangers for the separation of protein aggregates. J. Chromatogr. A 2009, 1216, 5256-5264.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5256-5264
    • Suda, E.J.1    Thomas, K.E.2    Pabst, T.M.3    Mensah, P.4
  • 23
    • 0037223763 scopus 로고    scopus 로고
    • A novel method for identifying PEGylation sites of protein using biotinylated PEG derivatives
    • DOI 10.1002/jps.10270
    • Lee, H., Park, T. G., A novel method for identifying PEGylation sites of protein using biotinylated PEG derivatives. J. Pharm. Sci. 2003, 92, 97-103. (Pubitemid 36042301)
    • (2003) Journal of Pharmaceutical Sciences , vol.92 , Issue.1 , pp. 97-103
    • Lee, H.1    Park, T.G.2
  • 24
    • 0021863999 scopus 로고
    • X-ray characterisation of an additional binding site in lysozyme
    • DOI 10.1016/0014-5793(85)80701-8
    • Veerapandian, B., Salunke, D. M., Vijayan, M., X-ray characterisation of an additional binding site in lysozyme. FEBS Lett. 1985, 186, 163-167. (Pubitemid 15070298)
    • (1985) FEBS Letters , vol.186 , Issue.2 , pp. 163-167
    • Veerapandian, B.1    Salunke, D.M.2    Vijayan, M.3
  • 25
    • 77952160600 scopus 로고    scopus 로고
    • Changes in retention behavior of fluorescently labeled proteins during ion-exchange chromatography caused by different protein surface labeling positions
    • Teske, C. A., Simon, R., Niebisch, A., Hubbuch, J., Changes in retention behavior of fluorescently labeled proteins during ion-exchange chromatography caused by different protein surface labeling positions. Biotechnol. Bioeng. 2007, 96, 57-66.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 57-66
    • Teske, C.A.1    Simon, R.2    Niebisch, A.3    Hubbuch, J.4
  • 26
    • 34247199425 scopus 로고    scopus 로고
    • A novel approach to characterize the binding orientation of lysozyme on ion-exchange resins
    • DOI 10.1016/j.chroma.2007.03.074, PII S0021967307005778
    • Dismer, F., Hubbuch, J., A novel approach to characterize the binding orientation of lysozyme on ion-exchange resins. J. Chromatogr. A 2007, 1149, 312-320. (Pubitemid 46627656)
    • (2007) Journal of Chromatography a , vol.1149 , Issue.2 , pp. 312-320
    • Dismer, F.1    Hubbuch, J.2
  • 27
    • 44349133384 scopus 로고    scopus 로고
    • Effects of ionic strength and mobile phase pH on the binding orientation of lysozyme on different ion-exchange adsorbents
    • Dismer, F., Petzold, M., Hubbuch, J., Effects of ionic strength and mobile phase pH on the binding orientation of lysozyme on different ion-exchange adsorbents. J. Chromatogr. A 2008, 1194, 11-21.
    • (2008) J. Chromatogr. A , vol.1194 , pp. 11-21
    • Dismer, F.1    Petzold, M.2    Hubbuch, J.3
  • 28
    • 36849064395 scopus 로고    scopus 로고
    • Solid-phase PEGylation of recombinant interferon a-2a for site-specific modification: Process performance, characterization, and in vitro bioactivity
    • DOI 10.1021/bc060245m
    • Byung, K. L., Jin, S. K., Hyung, J. K., Yamamoto, S., Lee, E. K., Solid-phase PEGylation of recombinant interferon a-2a for site-specific modification: Process performance, characterization, and in vitro bioactivity. Bioconj. Chem. 2007, 18, 1728-1734. (Pubitemid 350219969)
    • (2007) Bioconjugate Chemistry , vol.18 , Issue.6 , pp. 1728-1734
    • Byung, K.L.1    Jin, S.K.2    Hyung, J.K.3    Yamamoto, S.4    Lee, E.K.5


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