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Volumn 319, Issue 1-2, 2008, Pages 206-213

Ultrafiltration of PEGylated proteins: Fouling and concentration polarization effects

Author keywords

Concentration polarization; Membrane fouling; PEGylation; Ultrafiltration

Indexed keywords

CONCENTRATION (PROCESS); POLARIZATION; POLYMERIC MEMBRANES; ULTRAFILTRATION;

EID: 44249102502     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2008.03.035     Document Type: Article
Times cited : (50)

References (33)
  • 1
    • 0031118521 scopus 로고    scopus 로고
    • Strategies for the preparation and characterization of polyethylene glycol (PEG) conjugated pharmaceutical proteins
    • Fung W.J., Porter J.E., and Bailon P. Strategies for the preparation and characterization of polyethylene glycol (PEG) conjugated pharmaceutical proteins. Polym. Prepr. 38 1 (1997) 565-566
    • (1997) Polym. Prepr. , vol.38 , Issue.1 , pp. 565-566
    • Fung, W.J.1    Porter, J.E.2    Bailon, P.3
  • 2
    • 0017388651 scopus 로고    scopus 로고
    • Effect of covalent attachment of polyethylene-glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski A., McCoy J.R., Palczuk N.C., Vanes T., and Davis F.F. Effect of covalent attachment of polyethylene-glycol on immunogenicity and circulating life of bovine liver catalase. J. Biol. Chem. 252 11 (1997) 3582-3586
    • (1997) J. Biol. Chem. , vol.252 , Issue.11 , pp. 3582-3586
    • Abuchowski, A.1    McCoy, J.R.2    Palczuk, N.C.3    Vanes, T.4    Davis, F.F.5
  • 4
    • 27844515221 scopus 로고    scopus 로고
    • PEG-proteins: reaction engineering and separation issues
    • Fee C.J., and Van Alstine J.M. PEG-proteins: reaction engineering and separation issues. Chem. Eng. Sci. 61 (2006) 924-939
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 924-939
    • Fee, C.J.1    Van Alstine, J.M.2
  • 5
    • 0026549145 scopus 로고
    • Characterization of the heterogeneity of polyethylene glycol-modified superoxide dismutase by chromatographic and electrophoretic techniques
    • Snider J., Neville C., Yuan L.-C., and Bullock J. Characterization of the heterogeneity of polyethylene glycol-modified superoxide dismutase by chromatographic and electrophoretic techniques. J. Chromatogr. 599 1-2 (1992) 141-155
    • (1992) J. Chromatogr. , vol.599 , Issue.1-2 , pp. 141-155
    • Snider, J.1    Neville, C.2    Yuan, L.-C.3    Bullock, J.4
  • 6
    • 0027253357 scopus 로고
    • The conjugation of proteins with polyethylene-glycol and other polymers: altering properties of proteins to enhance their therapeutic potential
    • Katre N.V. The conjugation of proteins with polyethylene-glycol and other polymers: altering properties of proteins to enhance their therapeutic potential. Adv. Drug Deliv. Rev. 10 (1993) 91-114
    • (1993) Adv. Drug Deliv. Rev. , vol.10 , pp. 91-114
    • Katre, N.V.1
  • 7
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of viscosity radius and size exclusion chromatography behavior of PEGylated proteins
    • Fee C.J., and Van Alsine J.M. Prediction of viscosity radius and size exclusion chromatography behavior of PEGylated proteins. Bioconjug. Chem. 15 6 (2004) 1304-1313
    • (2004) Bioconjug. Chem. , vol.15 , Issue.6 , pp. 1304-1313
    • Fee, C.J.1    Van Alsine, J.M.2
  • 8
    • 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., and 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 908 (2001) 235-241
    • (2001) J. Chromatogr. A , vol.908 , pp. 235-241
    • Seely, J.E.1    Richey, C.W.2
  • 9
    • 33947502313 scopus 로고    scopus 로고
    • Comparison of strong anion-exchange for the purification of a PEGylated protein
    • Pabst T.M., Buckley J.J., Ramasubramanyan N., and Hunter A.K. Comparison of strong anion-exchange for the purification of a PEGylated protein. J. Chromatogr. A 1147 (2007) 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
  • 10
    • 33749369528 scopus 로고    scopus 로고
    • Ultrafiltration characteristics of PEGylated proteins
    • Molek J.R., and Zydney A.L. Ultrafiltration characteristics of PEGylated proteins. Biotech. Bioeng. 95 (2006) 474-482
    • (2006) Biotech. Bioeng. , vol.95 , pp. 474-482
    • Molek, J.R.1    Zydney, A.L.2
  • 11
    • 0028872640 scopus 로고
    • Buffer exchange using size exclusion chromatography, countercurrent dialysis, and tangential flow filtration: models, development, and industrial application
    • Kurnik R.T., Yu A.W., Blank G.S., Burton A.R., Smith D., Athalye A.M., and van Reis R. Buffer exchange using size exclusion chromatography, countercurrent dialysis, and tangential flow filtration: models, development, and industrial application. Biotech. Bioeng. 45 (1995) 149-157
    • (1995) Biotech. Bioeng. , vol.45 , pp. 149-157
    • Kurnik, R.T.1    Yu, A.W.2    Blank, G.S.3    Burton, A.R.4    Smith, D.5    Athalye, A.M.6    van Reis, R.7
  • 12
    • 0035889812 scopus 로고    scopus 로고
    • Ultrafiltration of protein and humic substances: effect of solution chemistry on fouling and flux decline
    • Jones K.L., and O'Melia C.R. Ultrafiltration of protein and humic substances: effect of solution chemistry on fouling and flux decline. J. Membr. Sci. 193 (2001) 163-173
    • (2001) J. Membr. Sci. , vol.193 , pp. 163-173
    • Jones, K.L.1    O'Melia, C.R.2
  • 13
    • 0020225075 scopus 로고
    • The effect of pH and ionic environment on the ultrafiltration of protein solutions with retentive membranes
    • Fane A.G., Fell C.J.D., and Suki A. The effect of pH and ionic environment on the ultrafiltration of protein solutions with retentive membranes. J. Membr. Sci. 16 (1983) 195-210
    • (1983) J. Membr. Sci. , vol.16 , pp. 195-210
    • Fane, A.G.1    Fell, C.J.D.2    Suki, A.3
  • 14
    • 0028519539 scopus 로고
    • Hydraulic permeability of protein deposits formed during microfiltration: effect of solution pH and ionic strength
    • Palecek S.P., and Zydney A.L. Hydraulic permeability of protein deposits formed during microfiltration: effect of solution pH and ionic strength. J. Membr. Sci. 95 (1994) 71-81
    • (1994) J. Membr. Sci. , vol.95 , pp. 71-81
    • Palecek, S.P.1    Zydney, A.L.2
  • 15
    • 0024681955 scopus 로고
    • Fouling of unmodified and modified polysulfone ultrafiltration membranes by ovalbumin
    • Nyström M. Fouling of unmodified and modified polysulfone ultrafiltration membranes by ovalbumin. J. Membr. Sci. 44 (1989) 183-196
    • (1989) J. Membr. Sci. , vol.44 , pp. 183-196
    • Nyström, M.1
  • 16
    • 0030604081 scopus 로고    scopus 로고
    • Preparation and investigation of chemically modified porous polyamide ultrafiltration membranes
    • Hosch J., and Staude E. Preparation and investigation of chemically modified porous polyamide ultrafiltration membranes. J. Membr. Sci. 121 (1996) 71-82
    • (1996) J. Membr. Sci. , vol.121 , pp. 71-82
    • Hosch, J.1    Staude, E.2
  • 17
    • 0020227891 scopus 로고
    • The role of macromolecular adsorption in fouling of ultrafiltration membranes
    • Matthiasson E. The role of macromolecular adsorption in fouling of ultrafiltration membranes. J. Membr. Sci. 16 (1983) 23-36
    • (1983) J. Membr. Sci. , vol.16 , pp. 23-36
    • Matthiasson, E.1
  • 18
    • 0027113652 scopus 로고
    • Transport and separation of proteins by ultrafiltration through sorptive and non-sorptive membranes
    • Nakatsuka S., and Michaels A.S. Transport and separation of proteins by ultrafiltration through sorptive and non-sorptive membranes. J. Membr. Sci. 69 (1992) 189-211
    • (1992) J. Membr. Sci. , vol.69 , pp. 189-211
    • Nakatsuka, S.1    Michaels, A.S.2
  • 19
    • 0026933684 scopus 로고
    • Determination of osmotic pressure and fouling resistance and their effects on performance of ultrafiltration membranes
    • Ko M.K., and Pellegrino J.J. Determination of osmotic pressure and fouling resistance and their effects on performance of ultrafiltration membranes. J. Membr. Sci. 74 (1992) 141-157
    • (1992) J. Membr. Sci. , vol.74 , pp. 141-157
    • Ko, M.K.1    Pellegrino, J.J.2
  • 20
    • 0031554626 scopus 로고    scopus 로고
    • Protein fouling during microfiltration: comparative behavior of different model proteins
    • Kelly S.T., and Zydney A.L. Protein fouling during microfiltration: comparative behavior of different model proteins. Biotech. Bioeng. 55 1 (1997) 91-100
    • (1997) Biotech. Bioeng. , vol.55 , Issue.1 , pp. 91-100
    • Kelly, S.T.1    Zydney, A.L.2
  • 21
    • 0027905923 scopus 로고
    • The influence of protein aggregates on the fouling of microfiltration membranes during stirred cell filtration
    • Kelly S.T., Opong W.S., and Zydney A.L. The influence of protein aggregates on the fouling of microfiltration membranes during stirred cell filtration. J. Membr. Sci. 80 (1993) 175-187
    • (1993) J. Membr. Sci. , vol.80 , pp. 175-187
    • Kelly, S.T.1    Opong, W.S.2    Zydney, A.L.3
  • 22
    • 0028858511 scopus 로고
    • Mechanisms for BSA fouling during microfiltration
    • Kelly S.T., and Zydney A.L. Mechanisms for BSA fouling during microfiltration. J. Membr. Sci. 107 (1995) 115-127
    • (1995) J. Membr. Sci. , vol.107 , pp. 115-127
    • Kelly, S.T.1    Zydney, A.L.2
  • 23
    • 0028485953 scopus 로고
    • Effects of intermolecular thiol-disulfide interchange reactions on BSA fouling during microfiltration
    • Kelly S.T., and Zydney A.L. Effects of intermolecular thiol-disulfide interchange reactions on BSA fouling during microfiltration. Biotech. Bioeng. 44 (1994) 972-982
    • (1994) Biotech. Bioeng. , vol.44 , pp. 972-982
    • Kelly, S.T.1    Zydney, A.L.2
  • 25
    • 0034237421 scopus 로고    scopus 로고
    • Buffer effects on the zeta potential of ultrafiltration membranes
    • Burns D.B., and Zydney A.L. Buffer effects on the zeta potential of ultrafiltration membranes. J. Membr. Sci. 172 (2000) 39-48
    • (2000) J. Membr. Sci. , vol.172 , pp. 39-48
    • Burns, D.B.1    Zydney, A.L.2
  • 26
    • 0032521883 scopus 로고    scopus 로고
    • Measurement of protein charge and ion binding using capillary electrophoresis
    • Menon M.K., and Zydney A.L. Measurement of protein charge and ion binding using capillary electrophoresis. Anal. Chem. 70 (1998) 1581-1584
    • (1998) Anal. Chem. , vol.70 , pp. 1581-1584
    • Menon, M.K.1    Zydney, A.L.2
  • 28
    • 29644434820 scopus 로고    scopus 로고
    • Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate
    • Hu T., Prabhakaran M., Acharya S.A., and Manjula B.N. Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate. Biochem. J. 392 (2005) 555-564
    • (2005) Biochem. J. , vol.392 , pp. 555-564
    • Hu, T.1    Prabhakaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 29
    • 33947368132 scopus 로고    scopus 로고
    • Synthesis and chromatographic separation of monomethoxypolyethylene glycol modified insulin
    • Zhang M., Zhang Y., Zhu S.-Y., Wu L.-F., and Dou H.-Z. Synthesis and chromatographic separation of monomethoxypolyethylene glycol modified insulin. Sep. Sci. Technol. 42 (2007) 789-801
    • (2007) Sep. Sci. Technol. , vol.42 , pp. 789-801
    • Zhang, M.1    Zhang, Y.2    Zhu, S.-Y.3    Wu, L.-F.4    Dou, H.-Z.5
  • 30
    • 0000031014 scopus 로고    scopus 로고
    • A comparison of polystyrene-poly(ethylene oxide) diblock copolymer and poly(ethylene oxide) homopolymer adsorption from aqueous solution
    • Pagac E.S., Prieve D.C., Solomentsev Y., and Tilton R.D. A comparison of polystyrene-poly(ethylene oxide) diblock copolymer and poly(ethylene oxide) homopolymer adsorption from aqueous solution. Langmuir 13 (1997) 2993-3001
    • (1997) Langmuir , vol.13 , pp. 2993-3001
    • Pagac, E.S.1    Prieve, D.C.2    Solomentsev, Y.3    Tilton, R.D.4
  • 31
    • 0033008246 scopus 로고    scopus 로고
    • Interaction between charged soft microcapsules and red blood cells: effects of pegylation of microcapsule membranes upon their surface properties
    • Makino K., Umetsu M., Goto Y., Nakayama A., Suhara T., Tsujii J., Kikuchi A., Ohshima H., Sakurai Y., and Okano T. Interaction between charged soft microcapsules and red blood cells: effects of pegylation of microcapsule membranes upon their surface properties. Colloids Surf. B 13 (1999) 287-297
    • (1999) Colloids Surf. B , vol.13 , pp. 287-297
    • Makino, K.1    Umetsu, M.2    Goto, Y.3    Nakayama, A.4    Suhara, T.5    Tsujii, J.6    Kikuchi, A.7    Ohshima, H.8    Sakurai, Y.9    Okano, T.10
  • 32
    • 34548319514 scopus 로고    scopus 로고
    • A facile method for synthesis of pegylated polyethersulfone and its application in fabrication of antifouling ultrafiltration membrane
    • Shi Q., Su Y., Zhu S., Li C., Zhao Y., and Jiang Z. A facile method for synthesis of pegylated polyethersulfone and its application in fabrication of antifouling ultrafiltration membrane. J. Membr. Sci. 303 (2007) 204-212
    • (2007) J. Membr. Sci. , vol.303 , pp. 204-212
    • Shi, Q.1    Su, Y.2    Zhu, S.3    Li, C.4    Zhao, Y.5    Jiang, Z.6
  • 33
    • 0042698340 scopus 로고    scopus 로고
    • Synthesis of polyethylene glycol (PEG) derivatives and PEGylated-peptide biopolymer conjugates
    • Li J., and Kao W.J. Synthesis of polyethylene glycol (PEG) derivatives and PEGylated-peptide biopolymer conjugates. Biomacromolecules 4 (2003) 1055-1067
    • (2003) Biomacromolecules , vol.4 , pp. 1055-1067
    • Li, J.1    Kao, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.