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Volumn 45, Issue 3, 2009, Pages 232-238

Application of dye-ligands affinity adsorbent in capturing of rabbit immunoglobulin G

Author keywords

Adsorption; Affinity; Bioseparation; Dye ligand; Expanded bed chromatography; Immunoglobulin G purification

Indexed keywords

AFFINITY; BIOSEPARATION; DYE-LIGAND; EXPANDED BED CHROMATOGRAPHY; IMMUNOGLOBULIN G PURIFICATION;

EID: 67349182598     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2009.04.003     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 0000100701 scopus 로고
    • Simultaneous separation and purification of pyruvate kinase and lactate dehydrogenase by dye-ligand chromatography
    • Makriyannis T., and Clonis Y.D. Simultaneous separation and purification of pyruvate kinase and lactate dehydrogenase by dye-ligand chromatography. Process Biochem. 28 (1993) 179-185
    • (1993) Process Biochem. , vol.28 , pp. 179-185
    • Makriyannis, T.1    Clonis, Y.D.2
  • 2
    • 0037177117 scopus 로고    scopus 로고
    • Procion Green H-4G immobilized on a new IPN hydrogel poly(2-hydroxyethylmethacrylate)/chitosan: preparation and its application to the adsorption of lysozyme
    • Bayramoǧlu G., and Arica M.Y. Procion Green H-4G immobilized on a new IPN hydrogel poly(2-hydroxyethylmethacrylate)/chitosan: preparation and its application to the adsorption of lysozyme. Colloids Surf. 202 (2002) 41-52
    • (2002) Colloids Surf. , vol.202 , pp. 41-52
    • Bayramoǧlu, G.1    Arica, M.Y.2
  • 3
    • 0037454181 scopus 로고    scopus 로고
    • A predictive model for salt effects on the dye-ligand affinity adsorption equilibrium of protein
    • Zhang S., and Sun Y. A predictive model for salt effects on the dye-ligand affinity adsorption equilibrium of protein. Ind. Eng. Chem. Res. 42 (2003) 1235-1242
    • (2003) Ind. Eng. Chem. Res. , vol.42 , pp. 1235-1242
    • Zhang, S.1    Sun, Y.2
  • 4
    • 33750356645 scopus 로고    scopus 로고
    • Preparation of dye-ligand affinity chromatographic packings based on monodisperse poly(glycidylmethacrylate-co-ethylenedimetha-crylate) beads and their chromatographic properties
    • Wu F., Zhu Y., and Jia Z. Preparation of dye-ligand affinity chromatographic packings based on monodisperse poly(glycidylmethacrylate-co-ethylenedimetha-crylate) beads and their chromatographic properties. J. Chromatogr. A 1134 (2006) 45-50
    • (2006) J. Chromatogr. A , vol.1134 , pp. 45-50
    • Wu, F.1    Zhu, Y.2    Jia, Z.3
  • 5
    • 33750181623 scopus 로고    scopus 로고
    • Affinity separation of immunoglobulin G subclasses on dye attached poly(hydroxypropyl methacrylate) beads
    • Yavuz H., Akgöl S., Say R., and Denizli A. Affinity separation of immunoglobulin G subclasses on dye attached poly(hydroxypropyl methacrylate) beads. Int. J. Biol. Macromol. 39 (2006) 303-309
    • (2006) Int. J. Biol. Macromol. , vol.39 , pp. 303-309
    • Yavuz, H.1    Akgöl, S.2    Say, R.3    Denizli, A.4
  • 6
    • 33847326285 scopus 로고    scopus 로고
    • Dye-ligand expanded bed adsorption of G6PDH from highly dense unclarified yeast extract
    • Chow Y.M., Tey B.T., Ibrahim M.N., Ariff A., and Ling T.C. Dye-ligand expanded bed adsorption of G6PDH from highly dense unclarified yeast extract. Process Biochem. 42 (2007) 444-448
    • (2007) Process Biochem. , vol.42 , pp. 444-448
    • Chow, Y.M.1    Tey, B.T.2    Ibrahim, M.N.3    Ariff, A.4    Ling, T.C.5
  • 7
    • 0027006648 scopus 로고
    • Designer dyes: 'biomimetic' ligands for the purification of pharmaceutical proteins by affinity chromatography
    • Lowe C.R., Burton S.J., Burton N.P., Alderton W.K., Pitts J.M., and Thomas J.A. Designer dyes: 'biomimetic' ligands for the purification of pharmaceutical proteins by affinity chromatography. TIBTECH 10 (1992) 442-448
    • (1992) TIBTECH , vol.10 , pp. 442-448
    • Lowe, C.R.1    Burton, S.J.2    Burton, N.P.3    Alderton, W.K.4    Pitts, J.M.5    Thomas, J.A.6
  • 8
    • 0042756996 scopus 로고
    • Immobilized anthraquinone dyes for affinity chromatography
    • Beissner R.S., and Rudolph R.B. Immobilized anthraquinone dyes for affinity chromatography. J. Chromatogr. 161 (1978) 127-135
    • (1978) J. Chromatogr. , vol.161 , pp. 127-135
    • Beissner, R.S.1    Rudolph, R.B.2
  • 9
    • 0030664817 scopus 로고    scopus 로고
    • Adsorption-desorption of BSA to highly substituted dye-ligand adsorbent: quantitative study of the effect of ionic strength
    • He L.-Z., Gan Y.-R., and Sun Y. Adsorption-desorption of BSA to highly substituted dye-ligand adsorbent: quantitative study of the effect of ionic strength. Bioprocess Eng. 17 (1997) 301-305
    • (1997) Bioprocess Eng. , vol.17 , pp. 301-305
    • He, L.-Z.1    Gan, Y.-R.2    Sun, Y.3
  • 10
    • 0002151593 scopus 로고    scopus 로고
    • A diffusion model of protein and eluant for affinity filtration
    • He L.-Z., Dong X.-Y., and Sun Y. A diffusion model of protein and eluant for affinity filtration. Biochem. Eng. J. 2 (1998) 53-62
    • (1998) Biochem. Eng. J. , vol.2 , pp. 53-62
    • He, L.-Z.1    Dong, X.-Y.2    Sun, Y.3
  • 11
    • 0037204633 scopus 로고    scopus 로고
    • Steric mass-action model for dye-ligand affinity adsorption of protein
    • Zhang S., and Sun Y. Steric mass-action model for dye-ligand affinity adsorption of protein. J. Chromatogr. A 957 (2002) 89-97
    • (2002) J. Chromatogr. A , vol.957 , pp. 89-97
    • Zhang, S.1    Sun, Y.2
  • 12
    • 0041375244 scopus 로고    scopus 로고
    • Multivalent binding interaction of alcohol dehydrogenase on dye-metal affinity matrix
    • Hidayat C., Nakajima M., Takagi M., and Yoshida T. Multivalent binding interaction of alcohol dehydrogenase on dye-metal affinity matrix. J. Biosci. Bioeng. 96 (2003) 168-173
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 168-173
    • Hidayat, C.1    Nakajima, M.2    Takagi, M.3    Yoshida, T.4
  • 13
    • 0345743497 scopus 로고    scopus 로고
    • Protein separation with surfactant-coated polystyrene involving Cibacron Blue 3GA-conjugated Triton X-100
    • Saitoh T., Hattori N., and Hiraide M. Protein separation with surfactant-coated polystyrene involving Cibacron Blue 3GA-conjugated Triton X-100. J. Chromatogr. A 1028 (2004) 149-153
    • (2004) J. Chromatogr. A , vol.1028 , pp. 149-153
    • Saitoh, T.1    Hattori, N.2    Hiraide, M.3
  • 14
    • 20444417861 scopus 로고    scopus 로고
    • Process intensification of fluidized bed dye-ligand adsorption of G3PDH from unclarified disrupted yeast: a case study of the performance of a high-density steel-agarose pellicular adsorbent
    • Ling T.C., and Lyddiatt A. Process intensification of fluidized bed dye-ligand adsorption of G3PDH from unclarified disrupted yeast: a case study of the performance of a high-density steel-agarose pellicular adsorbent. Protein Expres. Purif. 42 (2005) 160-165
    • (2005) Protein Expres. Purif. , vol.42 , pp. 160-165
    • Ling, T.C.1    Lyddiatt, A.2
  • 15
    • 33947330124 scopus 로고    scopus 로고
    • A dye-ligand immobilized poly(2-hydroxyethylmethacrylate) membrane used for adsorption and isolation of immunoglobulin G
    • Bayramoǧlu G., Oktem H.A., and Arica M.Y. A dye-ligand immobilized poly(2-hydroxyethylmethacrylate) membrane used for adsorption and isolation of immunoglobulin G. Biochem. Eng. J. 34 (2007) 147-155
    • (2007) Biochem. Eng. J. , vol.34 , pp. 147-155
    • Bayramoǧlu, G.1    Oktem, H.A.2    Arica, M.Y.3
  • 16
    • 0037135353 scopus 로고    scopus 로고
    • Procion Brown MX-5BR attached and Lewis metals ion-immobilized poly(hydroxyethyl methacrylate)/chitosan IPNs membranes: their lysozyme adsorption equilibria and kinetics characterization
    • Bayramoǧlu G., Kaya B., and Arica M.Y. Procion Brown MX-5BR attached and Lewis metals ion-immobilized poly(hydroxyethyl methacrylate)/chitosan IPNs membranes: their lysozyme adsorption equilibria and kinetics characterization. Chem. Eng. Sci. 57 (2002) 2323-2334
    • (2002) Chem. Eng. Sci. , vol.57 , pp. 2323-2334
    • Bayramoǧlu, G.1    Kaya, B.2    Arica, M.Y.3
  • 17
    • 24044528574 scopus 로고    scopus 로고
    • Adsorption of serum albumin and γ-globulin from single and binary mixture and characterization of pHEMA-based affinity membrane surface by contact angle measurement
    • Bayramoǧlu G., Yalçin E., and Arica M.Y. Adsorption of serum albumin and γ-globulin from single and binary mixture and characterization of pHEMA-based affinity membrane surface by contact angle measurement. Biochem. Eng. J. 26 (2005) 12-21
    • (2005) Biochem. Eng. J. , vol.26 , pp. 12-21
    • Bayramoǧlu, G.1    Yalçin, E.2    Arica, M.Y.3
  • 19
    • 23044437213 scopus 로고    scopus 로고
    • Porous poly(hydroxyethyl methacrylate) based monolith as a new adsorbent for affinity chromatography
    • Uzan L., Say R., and Denizli A. Porous poly(hydroxyethyl methacrylate) based monolith as a new adsorbent for affinity chromatography. React. Funct. Polym. 64 (2005) 93-102
    • (2005) React. Funct. Polym. , vol.64 , pp. 93-102
    • Uzan, L.1    Say, R.2    Denizli, A.3
  • 20
  • 21
    • 33751080111 scopus 로고    scopus 로고
    • Immunoglobulin G adsorption behavior of l-histidine ligand attached and Lewis metal ions chelated affinity membranes
    • Bayramoǧlu G., Celik G., and Arica M.Y. Immunoglobulin G adsorption behavior of l-histidine ligand attached and Lewis metal ions chelated affinity membranes. Colloids Surf. A: Physicochem. Eng. Aspects 287 (2006) 75-85
    • (2006) Colloids Surf. A: Physicochem. Eng. Aspects , vol.287 , pp. 75-85
    • Bayramoǧlu, G.1    Celik, G.2    Arica, M.Y.3
  • 22
    • 33747125111 scopus 로고    scopus 로고
    • Effect of spacer-arm and Cu(II) ions on performance of l-histidine immobilized on poly(GMA/MMA) beads as an affinity ligand for separation and purification of IgG
    • Bayramoǧlu G., Senel A.U., and Arica M.Y. Effect of spacer-arm and Cu(II) ions on performance of l-histidine immobilized on poly(GMA/MMA) beads as an affinity ligand for separation and purification of IgG. Sep. Purif. Technol. 50 (2006) 229-239
    • (2006) Sep. Purif. Technol. , vol.50 , pp. 229-239
    • Bayramoǧlu, G.1    Senel, A.U.2    Arica, M.Y.3
  • 23
    • 34247342204 scopus 로고    scopus 로고
    • Newly synthesized bentonite-histidine (Bent-His) micro-composite affinity sorbents for IgG adsorption
    • Öztürk N., Tabak A., Akgöl S., and Denizli A. Newly synthesized bentonite-histidine (Bent-His) micro-composite affinity sorbents for IgG adsorption. Colloids Surf. A: Physicochem. Eng. Aspects 301 (2007) 490-497
    • (2007) Colloids Surf. A: Physicochem. Eng. Aspects , vol.301 , pp. 490-497
    • Öztürk, N.1    Tabak, A.2    Akgöl, S.3    Denizli, A.4
  • 24
    • 0018528183 scopus 로고
    • Protein purification using immobilized triazine dyes
    • Dean P.D.G., and Watson D.H. Protein purification using immobilized triazine dyes. J. Chromatogr. 165 (1979) 301-319
    • (1979) J. Chromatogr. , vol.165 , pp. 301-319
    • Dean, P.D.G.1    Watson, D.H.2
  • 25
    • 24944580008 scopus 로고    scopus 로고
    • Integration of mechanical cell disruption and fluidised bed recovery of G3PDH from unclarified disrupted yeast: a comparative study of the performance of unshielded and polymer shielded dye-ligand chromatography systems
    • Ling T.C., and Lyddiatt A. Integration of mechanical cell disruption and fluidised bed recovery of G3PDH from unclarified disrupted yeast: a comparative study of the performance of unshielded and polymer shielded dye-ligand chromatography systems. J. Biotechnol. 119 (2005) 436-448
    • (2005) J. Biotechnol. , vol.119 , pp. 436-448
    • Ling, T.C.1    Lyddiatt, A.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. 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
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 29
    • 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
    • Ng M.Y.T., Tan W.S., Abdullah N., Ling T.C., and Tey B.T. 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
  • 30
    • 34247114996 scopus 로고    scopus 로고
    • Characterization of BSA adsorption on mixed mode adsorbent I. Equilibrium study in a well-agitated contactor
    • Chang Y.-K., Chou S.-Y., Liu J.-L., and Tasi J.-C. Characterization of BSA adsorption on mixed mode adsorbent I. Equilibrium study in a well-agitated contactor. Biochem. Eng. J. 35 (2007) 56-65
    • (2007) Biochem. Eng. J. , vol.35 , pp. 56-65
    • Chang, Y.-K.1    Chou, S.-Y.2    Liu, J.-L.3    Tasi, J.-C.4
  • 31
    • 0000201598 scopus 로고
    • Effect of pH on the adsorption of immunoglobulin G on anionic poly(vinyltoluene) model latex particles
    • Bagchi P., and Birnbaum S.M. Effect of pH on the adsorption of immunoglobulin G on anionic poly(vinyltoluene) model latex particles. J. Colloid Interf. Sci. 83 (1981) 460-478
    • (1981) J. Colloid Interf. Sci. , vol.83 , pp. 460-478
    • Bagchi, P.1    Birnbaum, S.M.2
  • 32
    • 0031588738 scopus 로고    scopus 로고
    • Comparative studies on the isothermal characteristics of proteins adsorbed under batch equilibrium conditions to ion-exchange, immobilised metal ion affinity and dye affinity matrices with different ionic strength and temperature conditions
    • Finette G.M.S., Mao Q.-M., and Hearn M.T.W. Comparative studies on the isothermal characteristics of proteins adsorbed under batch equilibrium conditions to ion-exchange, immobilised metal ion affinity and dye affinity matrices with different ionic strength and temperature conditions. J. Chromatogr. A 763 (1997) 71-90
    • (1997) J. Chromatogr. A , vol.763 , pp. 71-90
    • Finette, G.M.S.1    Mao, Q.-M.2    Hearn, M.T.W.3
  • 33
    • 2942627782 scopus 로고    scopus 로고
    • Preparation and characterisation of surfaces properties of poly(hydroxyethylmethacrylate-co-methacrylolyamido-histidine) membranes: application for purification of human immunoglobulin G
    • Arica M.Y., Yalçin E., and Bayramoǧlu G. Preparation and characterisation of surfaces properties of poly(hydroxyethylmethacrylate-co-methacrylolyamido-histidine) membranes: application for purification of human immunoglobulin G. J. Chromatogr. B 807 (2004) 315-325
    • (2004) J. Chromatogr. B , vol.807 , pp. 315-325
    • Arica, M.Y.1    Yalçin, E.2    Bayramoǧlu, G.3
  • 35
    • 0035924114 scopus 로고    scopus 로고
    • Further studies on the contribution of electrostatic and hydrophobic interactions to protein adsorption on dye-ligand adsorbents
    • Zhang S., and Sun Y. Further studies on the contribution of electrostatic and hydrophobic interactions to protein adsorption on dye-ligand adsorbents. Biotechnol. Bioeng. 75 (2001) 710-717
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 710-717
    • Zhang, S.1    Sun, Y.2
  • 37
    • 0030624706 scopus 로고    scopus 로고
    • Fluidized bed adsorption as a primary recovery step in protein purification
    • Thömmes J. Fluidized bed adsorption as a primary recovery step in protein purification. Adv. Biochem. Eng. 58 (1997) 185-230
    • (1997) Adv. Biochem. Eng. , vol.58 , pp. 185-230
    • Thömmes, J.1
  • 38
    • 0029394832 scopus 로고
    • Development of an expanded bed technique for an affinity purification of G6PDH from unclarified yeast cell homogenates
    • Chang Y.K., McCreath G.E., and Chase H.A. Development of an expanded bed technique for an affinity purification of G6PDH from unclarified yeast cell homogenates. Biotechnol. Bioeng. 48 (1995) 355-366
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 355-366
    • Chang, Y.K.1    McCreath, G.E.2    Chase, H.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.