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Volumn 1844, Issue 11, 2014, Pages 1960-1969

Site-specific immobilization of recombinant antibody fragments through material-binding peptides for the sensitive detection of antigens in enzyme immunoassays

Author keywords

ELISA; Immobilization; Material binding peptide; Plastics

Indexed keywords

ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; PLASTIC; POLY(METHYL METHACRYLATE); POLYSTYRENE; RECOMBINANT ANTIBODY;

EID: 84907938891     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.07.007     Document Type: Review
Times cited : (32)

References (108)
  • 1
    • 0015116634 scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G
    • E. Engvall, and P. Perlmann Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G Immunochemistry 8 1971 871 874
    • (1971) Immunochemistry , vol.8 , pp. 871-874
    • Engvall, E.1    Perlmann, P.2
  • 2
    • 0015367077 scopus 로고
    • Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specific antibodies by enzyme-labeled anti-immunoglobulin in antigen-coated tubes
    • E. Engvall, and P. Perlmann Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specific antibodies by enzyme-labeled anti-immunoglobulin in antigen-coated tubes J. Immunol. 109 1972 129 135
    • (1972) J. Immunol. , vol.109 , pp. 129-135
    • Engvall, E.1    Perlmann, P.2
  • 3
    • 0036372462 scopus 로고    scopus 로고
    • Antibody-guided selection using capture-sandwich ELISA
    • K. Itoh, and T. Suzuki Antibody-guided selection using capture-sandwich ELISA Methods Mol. Biol. 178 2002 195 199
    • (2002) Methods Mol. Biol. , vol.178 , pp. 195-199
    • Itoh, K.1    Suzuki, T.2
  • 4
    • 0029915191 scopus 로고    scopus 로고
    • Oriented immobilization of antibodies and its applications in immunoassays and immunosensors
    • B. Lu, M.R. Smyth, and R. O'Kennedy Oriented immobilization of antibodies and its applications in immunoassays and immunosensors Analyst 121 1996 29R 32R
    • (1996) Analyst , vol.121 , pp. 29R-32R
    • Lu, B.1    Smyth, M.R.2    O'Kennedy, R.3
  • 5
    • 0026128969 scopus 로고
    • Adsorption of gamma-globulin, a model protein for antibody, on colloidal particles
    • A. Kondo, S. Oku, and K. Higashitani Adsorption of gamma-globulin, a model protein for antibody, on colloidal particles Biotechnol. Bioeng. 37 1991 537 543
    • (1991) Biotechnol. Bioeng. , vol.37 , pp. 537-543
    • Kondo, A.1    Oku, S.2    Higashitani, K.3
  • 6
    • 0035975883 scopus 로고    scopus 로고
    • The solid phase in affinity chromatography: Strategies for antibody attachment
    • M. Nisnevitch, and M.A. Firer The solid phase in affinity chromatography: strategies for antibody attachment J. Biochem. Biophys. Methods 49 2001 467 480
    • (2001) J. Biochem. Biophys. Methods , vol.49 , pp. 467-480
    • Nisnevitch, M.1    Firer, M.A.2
  • 8
    • 0031031232 scopus 로고    scopus 로고
    • Adsorption-induced antigenic changes and their significance in ELISA and immunological disorders
    • J.E. Butler, P. Navarro, and J. Sun Adsorption-induced antigenic changes and their significance in ELISA and immunological disorders Immunol. Investig. 26 1997 39 54
    • (1997) Immunol. Investig. , vol.26 , pp. 39-54
    • Butler, J.E.1    Navarro, P.2    Sun, J.3
  • 10
    • 44249089709 scopus 로고    scopus 로고
    • Dynamic adsorption of monoclonal antibody layers on hydrophilic silica surface: A combined study by spectroscopic ellipsometry and AFM
    • X. Wang, Y. Wang, H. Xu, H. Shan, and J.R. Lu Dynamic adsorption of monoclonal antibody layers on hydrophilic silica surface: a combined study by spectroscopic ellipsometry and AFM J. Colloid Interface Sci. 323 2008 18 25
    • (2008) J. Colloid Interface Sci. , vol.323 , pp. 18-25
    • Wang, X.1    Wang, Y.2    Xu, H.3    Shan, H.4    Lu, J.R.5
  • 11
    • 0020663769 scopus 로고
    • Principles, problems, and strategies in the use of antigenic mixtures for the enzyme-linked immunosorbent assay
    • G.E. Kenny, and C.L. Dunsmoor Principles, problems, and strategies in the use of antigenic mixtures for the enzyme-linked immunosorbent assay J. Clin. Microbiol. 17 1983 655 665
    • (1983) J. Clin. Microbiol. , vol.17 , pp. 655-665
    • Kenny, G.E.1    Dunsmoor, C.L.2
  • 13
    • 80054015249 scopus 로고    scopus 로고
    • Effect of antibody immobilization strategies on the analytical performance of a surface plasmon resonance-based immunoassay
    • S.K. Vashist, C.K. Dixit, B.D. MacCraith, and R. O'Kennedy Effect of antibody immobilization strategies on the analytical performance of a surface plasmon resonance-based immunoassay Analyst 136 2011 4431 4436
    • (2011) Analyst , vol.136 , pp. 4431-4436
    • Vashist, S.K.1    Dixit, C.K.2    Maccraith, B.D.3    O'Kennedy, R.4
  • 14
    • 3543113088 scopus 로고    scopus 로고
    • Latex immunoassays: Comparative studies on covalent and physical immobilization of antibodies. II. IgG
    • J.A. Molina-Bolivar, F. Galisteo-Gonzalez, and R. Hidalgo-Alvarez Latex immunoassays: comparative studies on covalent and physical immobilization of antibodies. II. IgG J. Biomater. Sci. Polym. Ed. 9 1998 1103 1113
    • (1998) J. Biomater. Sci. Polym. Ed. , vol.9 , pp. 1103-1113
    • Molina-Bolivar, J.A.1    Galisteo-Gonzalez, F.2    Hidalgo-Alvarez, R.3
  • 15
    • 0031713396 scopus 로고    scopus 로고
    • Latex immunoassays: Comparative studies on covalent and physical immobilization of antibodies. I. F(ab′)2 fragments
    • J.A. Molina-Bolivar, F. Galisteo-Gonzalez, and R. Hidalgo-Alvarez Latex immunoassays: comparative studies on covalent and physical immobilization of antibodies. I. F(ab′)2 fragments J. Biomater. Sci. Polym. Ed. 9 1998 1089 1101
    • (1998) J. Biomater. Sci. Polym. Ed. , vol.9 , pp. 1089-1101
    • Molina-Bolivar, J.A.1    Galisteo-Gonzalez, F.2    Hidalgo-Alvarez, R.3
  • 16
    • 0033990807 scopus 로고    scopus 로고
    • Assembling of engineered IgG-binding protein on gold surface for highly oriented antibody immobilization
    • S. Kanno, Y. Yanagida, T. Haruyama, E. Kobatake, and M. Aizawa Assembling of engineered IgG-binding protein on gold surface for highly oriented antibody immobilization J. Biotechnol. 76 2000 207 214
    • (2000) J. Biotechnol. , vol.76 , pp. 207-214
    • Kanno, S.1    Yanagida, Y.2    Haruyama, T.3    Kobatake, E.4    Aizawa, M.5
  • 17
    • 34250687970 scopus 로고    scopus 로고
    • Preparing a highly specific inert immunomolecular-magnetic beads for rapid detection and separation of S aureus and group G Streptococcus
    • X. Xiao, X. Yang, T. Liu, Z. Chen, L. Chen, H. Li, and L. Deng Preparing a highly specific inert immunomolecular-magnetic beads for rapid detection and separation of S. aureus and group G Streptococcus Appl. Microbiol. Biotechnol. 75 2007 1209 1216
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 1209-1216
    • Xiao, X.1    Yang, X.2    Liu, T.3    Chen, Z.4    Chen, L.5    Li, H.6    Deng, L.7
  • 18
    • 84870336195 scopus 로고    scopus 로고
    • ELP-z and ELP-zz capturing scaffolds for the purification of immunoglobulins by affinity precipitation
    • B. Madan, G. Chaudhary, S.M. Cramer, and W. Chen ELP-z and ELP-zz capturing scaffolds for the purification of immunoglobulins by affinity precipitation J. Biotechnol. 163 2013 10 16
    • (2013) J. Biotechnol. , vol.163 , pp. 10-16
    • Madan, B.1    Chaudhary, G.2    Cramer, S.M.3    Chen, W.4
  • 19
    • 61449147053 scopus 로고    scopus 로고
    • Photoactivable antibody binding protein: Site-selective and covalent coupling of antibody
    • Y. Jung, J.M. Lee, J.W. Kim, J. Yoon, H. Cho, and B.H. Chung Photoactivable antibody binding protein: site-selective and covalent coupling of antibody Anal. Chem. 81 2009 936 942
    • (2009) Anal. Chem. , vol.81 , pp. 936-942
    • Jung, Y.1    Lee, J.M.2    Kim, J.W.3    Yoon, J.4    Cho, H.5    Chung, B.H.6
  • 21
    • 0036366705 scopus 로고    scopus 로고
    • Overview of antibody phage-display technology and its applications
    • H.R. Hoogenboom Overview of antibody phage-display technology and its applications Methods Mol. Biol. 178 2002 1 37
    • (2002) Methods Mol. Biol. , vol.178 , pp. 1-37
    • Hoogenboom, H.R.1
  • 22
    • 0034285785 scopus 로고    scopus 로고
    • Phage display of antibody fragments
    • A. Pini, and L. Bracci Phage display of antibody fragments Curr. Protein Pept. Sci. 1 2000 155 169
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 155-169
    • Pini, A.1    Bracci, L.2
  • 23
    • 0036181477 scopus 로고    scopus 로고
    • Recombinant monoclonal antibody technology
    • D.L. Siegel Recombinant monoclonal antibody technology Transfus. Clin. Biol. 9 2002 15 22
    • (2002) Transfus. Clin. Biol. , vol.9 , pp. 15-22
    • Siegel, D.L.1
  • 24
    • 0028349880 scopus 로고
    • The genetic engineering of monoclonal antibodies
    • R.J. Owens, and R.J. Young The genetic engineering of monoclonal antibodies J. Immunol. Methods 168 1994 149 165
    • (1994) J. Immunol. Methods , vol.168 , pp. 149-165
    • Owens, R.J.1    Young, R.J.2
  • 25
    • 0027347133 scopus 로고
    • Antibody engineering using Escherichia coli as host
    • E.S. Ward Antibody engineering using Escherichia coli as host Adv. Pharmacol. 24 1993 1 20
    • (1993) Adv. Pharmacol. , vol.24 , pp. 1-20
    • Ward, E.S.1
  • 28
    • 70349736369 scopus 로고    scopus 로고
    • A single-step procedure of recombinant library construction for the selection of efficiently produced llama VH binders directed against cancer markers
    • D. Kastelic, S. Frkovic-Grazio, D. Baty, G. Truan, R. Komel, and D. Pompon A single-step procedure of recombinant library construction for the selection of efficiently produced llama VH binders directed against cancer markers J. Immunol. Methods 350 2009 54 62
    • (2009) J. Immunol. Methods , vol.350 , pp. 54-62
    • Kastelic, D.1    Frkovic-Grazio, S.2    Baty, D.3    Truan, G.4    Komel, R.5    Pompon, D.6
  • 29
    • 59949088708 scopus 로고    scopus 로고
    • Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression
    • R. Klooster, M.R. Eman, Q. le Duc, P. Verheesen, C.T. Verrips, R.C. Roovers, and J.A. Post Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression J. Immunol. Methods 342 2009 1 12
    • (2009) J. Immunol. Methods , vol.342 , pp. 1-12
    • Klooster, R.1    Eman, M.R.2    Le Duc, Q.3    Verheesen, P.4    Verrips, C.T.5    Roovers, R.C.6    Post, J.A.7
  • 30
  • 32
    • 76749096306 scopus 로고    scopus 로고
    • Functional expression of single-chain Fv antibody in the cytoplasm of Escherichia coli by thioredoxin fusion and co-expression of molecular chaperones
    • H. Sonoda, Y. Kumada, T. Katsuda, and H. Yamaji Functional expression of single-chain Fv antibody in the cytoplasm of Escherichia coli by thioredoxin fusion and co-expression of molecular chaperones Protein Expr. Purif. 70 2010 248 253
    • (2010) Protein Expr. Purif. , vol.70 , pp. 248-253
    • Sonoda, H.1    Kumada, Y.2    Katsuda, T.3    Yamaji, H.4
  • 33
    • 37049021103 scopus 로고    scopus 로고
    • Production of single-chain variable fragment antibody (scFv) in fed-batch and continuous culture of Pichia pastoris by two different methanol feeding methods
    • S. Yamawaki, T. Matsumoto, Y. Ohnishi, Y. Kumada, N. Shiomi, T. Katsuda, E.K. Lee, and S. Katoh Production of single-chain variable fragment antibody (scFv) in fed-batch and continuous culture of Pichia pastoris by two different methanol feeding methods J. Biosci. Bioeng. 104 2007 403 407
    • (2007) J. Biosci. Bioeng. , vol.104 , pp. 403-407
    • Yamawaki, S.1    Matsumoto, T.2    Ohnishi, Y.3    Kumada, Y.4    Shiomi, N.5    Katsuda, T.6    Lee, E.K.7    Katoh, S.8
  • 35
    • 33744499696 scopus 로고    scopus 로고
    • Engineering of Pichia pastoris for improved production of antibody fragments
    • B. Gasser, M. Maurer, J. Gach, R. Kunert, and D. Mattanovich Engineering of Pichia pastoris for improved production of antibody fragments Biotechnol. Bioeng. 94 2006 353 361
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 353-361
    • Gasser, B.1    Maurer, M.2    Gach, J.3    Kunert, R.4    Mattanovich, D.5
  • 37
    • 0032479180 scopus 로고    scopus 로고
    • Expression of an antibody fragment at high levels in the bacterial cytoplasm
    • P. Martineau, P. Jones, and G. Winter Expression of an antibody fragment at high levels in the bacterial cytoplasm J. Mol. Biol. 280 1998 117 127
    • (1998) J. Mol. Biol. , vol.280 , pp. 117-127
    • Martineau, P.1    Jones, P.2    Winter, G.3
  • 38
    • 84872177505 scopus 로고    scopus 로고
    • Production of single chain fragment variable (scFv) antibodies in Escherichia coli using the LEX bioreactor
    • S. Miethe, T. Meyer, S. Wohl-Bruhn, A. Frenzel, T. Schirrmann, S. Dubel, and M. Hust Production of single chain fragment variable (scFv) antibodies in Escherichia coli using the LEX bioreactor J. Biotechnol. 163 2013 105 111
    • (2013) J. Biotechnol. , vol.163 , pp. 105-111
    • Miethe, S.1    Meyer, T.2    Wohl-Bruhn, S.3    Frenzel, A.4    Schirrmann, T.5    Dubel, S.6    Hust, M.7
  • 41
    • 0032448966 scopus 로고    scopus 로고
    • High-density immobilization of an antibody fragment to a carboxymethylated dextran-linked biosensor surface
    • S. Howell, M. Kenmore, M. Kirkland, and R.A. Badley High-density immobilization of an antibody fragment to a carboxymethylated dextran-linked biosensor surface J. Mol. Recognit. 11 1998 200 203
    • (1998) J. Mol. Recognit. , vol.11 , pp. 200-203
    • Howell, S.1    Kenmore, M.2    Kirkland, M.3    Badley, R.A.4
  • 42
    • 0029609864 scopus 로고
    • Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies
    • I. Kurucz, J.A. Titus, C.R. Jost, and D.M. Segal Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies Mol. Immunol. 32 1995 1443 1452
    • (1995) Mol. Immunol. , vol.32 , pp. 1443-1452
    • Kurucz, I.1    Titus, J.A.2    Jost, C.R.3    Segal, D.M.4
  • 44
    • 41449093106 scopus 로고    scopus 로고
    • Engineering peptide linkers for scFv immunosensors
    • Z. Shen, H. Yan, Y. Zhang, R.L. Mernaugh, and X. Zeng Engineering peptide linkers for scFv immunosensors Anal. Chem. 80 2008 1910 1917
    • (2008) Anal. Chem. , vol.80 , pp. 1910-1917
    • Shen, Z.1    Yan, H.2    Zhang, Y.3    Mernaugh, R.L.4    Zeng, X.5
  • 45
    • 77953317927 scopus 로고    scopus 로고
    • Direct observation of adsorption-induced inactivation of antibody fragments surrounded by mixed-PEG layer on a gold surface
    • K. Yoshimoto, M. Nishio, H. Sugasawa, and Y. Nagasaki Direct observation of adsorption-induced inactivation of antibody fragments surrounded by mixed-PEG layer on a gold surface J. Am. Chem. Soc. 132 2010 7982 7989
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7982-7989
    • Yoshimoto, K.1    Nishio, M.2    Sugasawa, H.3    Nagasaki, Y.4
  • 46
    • 53249115573 scopus 로고    scopus 로고
    • Recent advances in controlled immobilization of proteins onto the surface of the solid substrate and its possible application to proteomics
    • K. Nakanishi, Y. Kumada, K. Imamura, and H. Imanaka Recent advances in controlled immobilization of proteins onto the surface of the solid substrate and its possible application to proteomics Curr. Proteomics 5 2008 161 175
    • (2008) Curr. Proteomics , vol.5 , pp. 161-175
    • Nakanishi, K.1    Kumada, Y.2    Imamura, K.3    Imanaka, H.4
  • 47
    • 28144437795 scopus 로고    scopus 로고
    • Protein engineering strategies for selective protein purification
    • M. Hedhammar, and S. Hober Protein engineering strategies for selective protein purification Chem. Eng. Technol. 28 2005 1315 1325
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1315-1325
    • Hedhammar, M.1    Hober, S.2
  • 48
    • 0023920896 scopus 로고
    • Large-scale chromatography of recombinant proteins
    • E. Hochuli Large-scale chromatography of recombinant proteins J. Chromatogr. 444 1988 293 302
    • (1988) J. Chromatogr. , vol.444 , pp. 293-302
    • Hochuli, E.1
  • 49
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • J. Porath, J. Carlsson, I. Olsson, and G. Belfrage Metal chelate affinity chromatography, a new approach to protein fractionation Nature 258 1975 598 599
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 50
    • 77956924836 scopus 로고    scopus 로고
    • Electrochemical detection of D-dimer as deep vein thrombosis marker using single-chain D-dimer antibody immobilized on functionalized polypyrrole
    • S. Chebil, I. Hafaiedh, H. Sauriat-Dorizon, N. Jaffrezic-Renault, A. Errachid, Z. Ali, and H. Korri-Youssoufi Electrochemical detection of D-dimer as deep vein thrombosis marker using single-chain D-dimer antibody immobilized on functionalized polypyrrole Biosens. Bioelectron. 26 2010 736 742
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 736-742
    • Chebil, S.1    Hafaiedh, I.2    Sauriat-Dorizon, H.3    Jaffrezic-Renault, N.4    Errachid, A.5    Ali, Z.6    Korri-Youssoufi, H.7
  • 51
    • 84876251486 scopus 로고    scopus 로고
    • Design, production, and characterization of a single-chain variable fragment (ScFv) derived from the prostate specific membrane antigen (PSMA) monoclonal antibody J591
    • S.A. Parker, I.L. Diaz, K.A. Anderson, and C.A. Batt Design, production, and characterization of a single-chain variable fragment (ScFv) derived from the prostate specific membrane antigen (PSMA) monoclonal antibody J591 Protein Expr. Purif. 89 2013 136 145
    • (2013) Protein Expr. Purif. , vol.89 , pp. 136-145
    • Parker, S.A.1    Diaz, I.L.2    Anderson, K.A.3    Batt, C.A.4
  • 53
    • 28844456139 scopus 로고    scopus 로고
    • Efficient recovery of the functional IP10-scFv fusion protein from inclusion bodies with an on-column refolding system
    • J.Q. Guo, Q.M. Li, J.Y. Zhou, G.P. Zhang, Y.Y. Yang, G.X. Xing, D. Zhao, S.Y. You, and C.Y. Zhang Efficient recovery of the functional IP10-scFv fusion protein from inclusion bodies with an on-column refolding system Protein Expr. Purif. 45 2006 168 174
    • (2006) Protein Expr. Purif. , vol.45 , pp. 168-174
    • Guo, J.Q.1    Li, Q.M.2    Zhou, J.Y.3    Zhang, G.P.4    Yang, Y.Y.5    Xing, G.X.6    Zhao, D.7    You, S.Y.8    Zhang, C.Y.9
  • 54
    • 0037464405 scopus 로고    scopus 로고
    • Construction and high-level expression of a single-chain Fv antibody fragment specific for acidic isoferritin in Escherichia coli
    • J.Q. Guo, S.Y. You, L. Li, Y.Z. Zhang, J.N. Huang, and C.Y. Zhang Construction and high-level expression of a single-chain Fv antibody fragment specific for acidic isoferritin in Escherichia coli J. Biotechnol. 102 2003 177 189
    • (2003) J. Biotechnol. , vol.102 , pp. 177-189
    • Guo, J.Q.1    You, S.Y.2    Li, L.3    Zhang, Y.Z.4    Huang, J.N.5    Zhang, C.Y.6
  • 55
    • 73249153396 scopus 로고    scopus 로고
    • Oriented immobilization of antibody fragments on Ni-decorated single-walled carbon nanotube devices
    • Y.S. Lo, D.H. Nam, H.M. So, H. Chang, J.J. Kim, Y.H. Kim, and J.O. Lee Oriented immobilization of antibody fragments on Ni-decorated single-walled carbon nanotube devices ACS Nano 3 2009 3649 3655
    • (2009) ACS Nano , vol.3 , pp. 3649-3655
    • Lo, Y.S.1    Nam, D.H.2    So, H.M.3    Chang, H.4    Kim, J.J.5    Kim, Y.H.6    Lee, J.O.7
  • 56
    • 0029146150 scopus 로고
    • Cloning vectors for the production of proteins in Dictyostelium discoideum
    • D.J. Manstein, H.P. Schuster, P. Morandini, and D.M. Hunt Cloning vectors for the production of proteins in Dictyostelium discoideum Gene 162 1995 129 134
    • (1995) Gene , vol.162 , pp. 129-134
    • Manstein, D.J.1    Schuster, H.P.2    Morandini, P.3    Hunt, D.M.4
  • 57
    • 0027499708 scopus 로고
    • The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment
    • T.G. Schmidt, and A. Skerra The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment Protein Eng. 6 1993 109 122
    • (1993) Protein Eng. , vol.6 , pp. 109-122
    • Schmidt, T.G.1    Skerra, A.2
  • 58
    • 0032524072 scopus 로고    scopus 로고
    • Strep-tag II affinity purification: An approach to study intermediates of metalloenzyme biosynthesis
    • T. Maier, N. Drapal, M. Thanbichler, and A. Bock Strep-tag II affinity purification: an approach to study intermediates of metalloenzyme biosynthesis Anal. Biochem. 259 1998 68 73
    • (1998) Anal. Biochem. , vol.259 , pp. 68-73
    • Maier, T.1    Drapal, N.2    Thanbichler, M.3    Bock, A.4
  • 61
    • 0036364574 scopus 로고    scopus 로고
    • Cloning, functional expression and kinetic characterization of pesticide-selective Fab fragment variants derived by molecular evolution of variable antibody genes
    • D. Rau, K. Kramer, and B. Hock Cloning, functional expression and kinetic characterization of pesticide-selective Fab fragment variants derived by molecular evolution of variable antibody genes Anal. Bioanal. Chem. 372 2002 261 267
    • (2002) Anal. Bioanal. Chem. , vol.372 , pp. 261-267
    • Rau, D.1    Kramer, K.2    Hock, B.3
  • 62
    • 0027312336 scopus 로고
    • Bacterial expression of immunoglobulin fragments
    • A. Skerra Bacterial expression of immunoglobulin fragments Curr. Opin. Immunol. 5 1993 256 262
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 256-262
    • Skerra, A.1
  • 63
    • 0034452793 scopus 로고    scopus 로고
    • Cloning and expression in Pichia pastoris of a genetically engineered single chain antibody against the rat transferrin receptor
    • R.J. Boado, A. Ji, and W.M. Pardridge Cloning and expression in Pichia pastoris of a genetically engineered single chain antibody against the rat transferrin receptor J. Drug Target. 8 2000 403 412
    • (2000) J. Drug Target. , vol.8 , pp. 403-412
    • Boado, R.J.1    Ji, A.2    Pardridge, W.M.3
  • 64
    • 58549105076 scopus 로고    scopus 로고
    • High-level expression of a functional humanized anti-CTLA4 single-chain variable fragment antibody in Pichia pastoris
    • H. Cai, L. Chen, L. Wan, L. Zeng, H. Yang, S. Li, Y. Li, J. Cheng, and X. Lu High-level expression of a functional humanized anti-CTLA4 single-chain variable fragment antibody in Pichia pastoris Appl. Microbiol. Biotechnol. 82 2009 41 48
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 41-48
    • Cai, H.1    Chen, L.2    Wan, L.3    Zeng, L.4    Yang, H.5    Li, S.6    Li, Y.7    Cheng, J.8    Lu, X.9
  • 67
    • 84934440276 scopus 로고    scopus 로고
    • Pichia surface display: A tool for screening single domain antibodies
    • K. De Schutter, and N. Callewaert Pichia surface display: a tool for screening single domain antibodies Methods Mol. Biol. 911 2012 125 134
    • (2012) Methods Mol. Biol. , vol.911 , pp. 125-134
    • De Schutter, K.1    Callewaert, N.2
  • 68
    • 79953681894 scopus 로고    scopus 로고
    • Single-chain antibody fragment production in Pichia pastoris: Benefits of prolonged pre-induction glycerol feeding
    • N.K. Khatri, D. Gocke, O. Trentmann, P. Neubauer, and F. Hoffmann Single-chain antibody fragment production in Pichia pastoris: benefits of prolonged pre-induction glycerol feeding Biotechnol. J. 6 2011 452 462
    • (2011) Biotechnol. J. , vol.6 , pp. 452-462
    • Khatri, N.K.1    Gocke, D.2    Trentmann, O.3    Neubauer, P.4    Hoffmann, F.5
  • 70
    • 0032706361 scopus 로고    scopus 로고
    • A single chain Fv specific against Western equine encephalitis virus
    • B. Xu, J. Kriangkum, L.P. Nagata, R.E. Fulton, and M.R. Suresh A single chain Fv specific against Western equine encephalitis virus Hybridoma 18 1999 315 323
    • (1999) Hybridoma , vol.18 , pp. 315-323
    • Xu, B.1    Kriangkum, J.2    Nagata, L.P.3    Fulton, R.E.4    Suresh, M.R.5
  • 73
    • 5444244426 scopus 로고    scopus 로고
    • Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability
    • D. Kase, J.L. Kulp III, M. Yudasaka, J.S. Evans, S. Iijima, and K. Shiba Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability Langmuir 20 2004 8939 8941
    • (2004) Langmuir , vol.20 , pp. 8939-8941
    • Kase, D.1    Kulp, J.L.2    Yudasaka, M.3    Evans, J.S.4    Iijima, S.5    Shiba, K.6
  • 74
    • 16244366831 scopus 로고    scopus 로고
    • Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1)
    • K. Sano, H. Sasaki, and K. Shiba Specificity and biomineralization activities of Ti-binding peptide-1 (TBP-1) Langmuir 21 2005 3090 3095
    • (2005) Langmuir , vol.21 , pp. 3090-3095
    • Sano, K.1    Sasaki, H.2    Shiba, K.3
  • 75
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • K. Sano, and K. Shiba A hexapeptide motif that electrostatically binds to the surface of titanium J. Am. Chem. Soc. 125 2003 14234 14235
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14234-14235
    • Sano, K.1    Shiba, K.2
  • 76
    • 79957666651 scopus 로고    scopus 로고
    • Why does the silica-binding protein "si-tag" bind strongly to silica surfaces? Implications of conformational adaptation of the intrinsically disordered polypeptide to solid surfaces
    • T. Ikeda, and A. Kuroda Why does the silica-binding protein "Si-tag" bind strongly to silica surfaces? Implications of conformational adaptation of the intrinsically disordered polypeptide to solid surfaces Colloids Surf. B: Biointerfaces 86 2011 359 363
    • (2011) Colloids Surf. B: Biointerfaces , vol.86 , pp. 359-363
    • Ikeda, T.1    Kuroda, A.2
  • 77
    • 79952627013 scopus 로고    scopus 로고
    • The silica-binding Si-tag functions as an affinity tag even under denaturing conditions
    • T. Ikeda, K. Motomura, Y. Agou, T. Ishida, R. Hirota, and A. Kuroda The silica-binding Si-tag functions as an affinity tag even under denaturing conditions Protein Expr. Purif. 77 2011 173 177
    • (2011) Protein Expr. Purif. , vol.77 , pp. 173-177
    • Ikeda, T.1    Motomura, K.2    Agou, Y.3    Ishida, T.4    Hirota, R.5    Kuroda, A.6
  • 78
    • 77049094645 scopus 로고    scopus 로고
    • Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner
    • T. Ikeda, K. Ninomiya, R. Hirota, and A. Kuroda Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner Protein Expr. Purif. 71 2010 91 95
    • (2010) Protein Expr. Purif. , vol.71 , pp. 91-95
    • Ikeda, T.1    Ninomiya, K.2    Hirota, R.3    Kuroda, A.4
  • 81
    • 47349131273 scopus 로고    scopus 로고
    • Biological selection of peptides for poly(l-lactide) substrates
    • H. Matsuno, J. Sekine, H. Yajima, and T. Serizawa Biological selection of peptides for poly(l-lactide) substrates Langmuir 24 2008 6399 6403
    • (2008) Langmuir , vol.24 , pp. 6399-6403
    • Matsuno, H.1    Sekine, J.2    Yajima, H.3    Serizawa, T.4
  • 82
    • 35948972439 scopus 로고    scopus 로고
    • Highly specific affinities of short peptides against synthetic polymers
    • T. Serizawa, T. Sawada, and H. Matsuno Highly specific affinities of short peptides against synthetic polymers Langmuir 23 2007 11127 11133
    • (2007) Langmuir , vol.23 , pp. 11127-11133
    • Serizawa, T.1    Sawada, T.2    Matsuno, H.3
  • 84
    • 58149352336 scopus 로고    scopus 로고
    • A novel affinity ligand for polystyrene surface from a phage display random library and its application in anti-HIV-1 ELISA system
    • B. Feng, Y. Dai, L. Wang, N. Tao, S. Huang, and H. Zeng A novel affinity ligand for polystyrene surface from a phage display random library and its application in anti-HIV-1 ELISA system Biologicals 37 2009 48 54
    • (2009) Biologicals , vol.37 , pp. 48-54
    • Feng, B.1    Dai, Y.2    Wang, L.3    Tao, N.4    Huang, S.5    Zeng, H.6
  • 85
    • 33646023149 scopus 로고    scopus 로고
    • Screening and characterization of affinity peptide tags specific to polystyrene supports for the orientated immobilization of proteins
    • Y. Kumada, Y. Tokunaga, H. Imanaka, K. Imamura, T. Sakiyama, S. Katoh, and K. Nakanishi Screening and characterization of affinity peptide tags specific to polystyrene supports for the orientated immobilization of proteins Biotechnol. Prog. 22 2006 401 405
    • (2006) Biotechnol. Prog. , vol.22 , pp. 401-405
    • Kumada, Y.1    Tokunaga, Y.2    Imanaka, H.3    Imamura, K.4    Sakiyama, T.5    Katoh, S.6    Nakanishi, K.7
  • 86
    • 70350119793 scopus 로고    scopus 로고
    • High biological activity of a recombinant protein immobilized onto polystyrene
    • Y. Kumada, Y. Shiritani, K. Hamasaki, T. Ohse, and M. Kishimoto High biological activity of a recombinant protein immobilized onto polystyrene Biotechnol. J. 4 2009 1178 1189
    • (2009) Biotechnol. J. , vol.4 , pp. 1178-1189
    • Kumada, Y.1    Shiritani, Y.2    Hamasaki, K.3    Ohse, T.4    Kishimoto, M.5
  • 87
    • 77952101293 scopus 로고    scopus 로고
    • Characterization of polystyrene-binding peptides (PS-tags) for site-specific immobilization of proteins
    • Y. Kumada, D. Kuroki, H. Yasui, T. Ohse, and M. Kishimoto Characterization of polystyrene-binding peptides (PS-tags) for site-specific immobilization of proteins J. Biosci. Bioeng. 109 2010 583 587
    • (2010) J. Biosci. Bioeng. , vol.109 , pp. 583-587
    • Kumada, Y.1    Kuroki, D.2    Yasui, H.3    Ohse, T.4    Kishimoto, M.5
  • 88
    • 84864062214 scopus 로고    scopus 로고
    • Screening of PC and PMMA-binding peptides for site-specific immobilization of proteins
    • Y. Kumada, S. Murata, Y. Ishikawa, K. Nakatsuka, and M. Kishimoto Screening of PC and PMMA-binding peptides for site-specific immobilization of proteins J. Biotechnol. 160 2012 222 228
    • (2012) J. Biotechnol. , vol.160 , pp. 222-228
    • Kumada, Y.1    Murata, S.2    Ishikawa, Y.3    Nakatsuka, K.4    Kishimoto, M.5
  • 89
    • 84901823239 scopus 로고    scopus 로고
    • Identification and characterization of peptide fragments for the direct and site-specific immobilization of functional proteins onto the surface of silicon nitride
    • Y. Kumada, T. Ootsuka, M. Asada, S. Yoshizuka, M. Chiyama, M. Sakane, H.M. Fida, K. Sawada, K. Okumura, and M. Kishimoto Identification and characterization of peptide fragments for the direct and site-specific immobilization of functional proteins onto the surface of silicon nitride J. Biotechnol. 184C 2014 103 110
    • (2014) J. Biotechnol. , vol.184 C , pp. 103-110
    • Kumada, Y.1    Ootsuka, T.2    Asada, M.3    Yoshizuka, S.4    Chiyama, M.5    Sakane, M.6    Fida, H.M.7    Sawada, K.8    Okumura, K.9    Kishimoto, M.10
  • 90
    • 84857308609 scopus 로고    scopus 로고
    • Increased affinity and solubility of peptides used for direct peptide ELISA on polystyrene surfaces through fusion with a polystyrene-binding peptide tag
    • J.M. Kogot, D.A. Sarkes, I. Val-Addo, P.M. Pellegrino, and D.N. Stratis-Cullum Increased affinity and solubility of peptides used for direct peptide ELISA on polystyrene surfaces through fusion with a polystyrene-binding peptide tag Biotechniques 52 2012 95 102
    • (2012) Biotechniques , vol.52 , pp. 95-102
    • Kogot, J.M.1    Sarkes, D.A.2    Val-Addo, I.3    Pellegrino, P.M.4    Stratis-Cullum, D.N.5
  • 91
    • 78649450819 scopus 로고    scopus 로고
    • Design of culture substrates for large-scale expansion of neural stem cells
    • S. Konagaya, K. Kato, T. Nakaji-Hirabayashi, and H. Iwata Design of culture substrates for large-scale expansion of neural stem cells Biomaterials 32 2011 992 1001
    • (2011) Biomaterials , vol.32 , pp. 992-1001
    • Konagaya, S.1    Kato, K.2    Nakaji-Hirabayashi, T.3    Iwata, H.4
  • 92
    • 84876718886 scopus 로고    scopus 로고
    • Well-oriented ZZ-PS-tag with high Fc-binding onto polystyrene surface for controlled immobilization of capture antibodies
    • J.B. Tang, X.F. Sun, H.M. Yang, B.G. Zhang, Z.J. Li, Z.J. Lin, and Z.Q. Gao Well-oriented ZZ-PS-tag with high Fc-binding onto polystyrene surface for controlled immobilization of capture antibodies Anal. Chim. Acta 776 2013 74 78
    • (2013) Anal. Chim. Acta , vol.776 , pp. 74-78
    • Tang, J.B.1    Sun, X.F.2    Yang, H.M.3    Zhang, B.G.4    Li, Z.J.5    Lin, Z.J.6    Gao, Z.Q.7
  • 93
    • 33846255071 scopus 로고    scopus 로고
    • Development of a one-step ELISA method using an affinity peptide tag specific to a hydrophilic polystyrene surface
    • Y. Kumada, S. Katoh, H. Imanaka, K. Imamura, and K. Nakanishi Development of a one-step ELISA method using an affinity peptide tag specific to a hydrophilic polystyrene surface J. Biotechnol. 127 2007 288 299
    • (2007) J. Biotechnol. , vol.127 , pp. 288-299
    • Kumada, Y.1    Katoh, S.2    Imanaka, H.3    Imamura, K.4    Nakanishi, K.5
  • 94
    • 36649028506 scopus 로고    scopus 로고
    • Characteristics of a liposome immunoassay on a poly(methyl methacrylate) surface
    • S.Y. Hwang, Y. Kumada, G.H. Seong, J. Choo, S. Katoh, and E.K. Lee Characteristics of a liposome immunoassay on a poly(methyl methacrylate) surface Anal. Bioanal. Chem. 389 2007 2251 2257
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 2251-2257
    • Hwang, S.Y.1    Kumada, Y.2    Seong, G.H.3    Choo, J.4    Katoh, S.5    Lee, E.K.6
  • 95
    • 67349139677 scopus 로고    scopus 로고
    • Efficient immobilization of a ligand antibody with high antigen-binding activity by use of a polystyrene-binding peptide and an intelligent microtiter plate
    • Y. Kumada, K. Hamasaki, Y. Shiritani, T. Ohse, and M. Kishimoto Efficient immobilization of a ligand antibody with high antigen-binding activity by use of a polystyrene-binding peptide and an intelligent microtiter plate J. Biotechnol. 142 2009 135 141
    • (2009) J. Biotechnol. , vol.142 , pp. 135-141
    • Kumada, Y.1    Hamasaki, K.2    Shiritani, Y.3    Ohse, T.4    Kishimoto, M.5
  • 96
    • 33846040689 scopus 로고    scopus 로고
    • Protein-protein interaction analysis using an affinity peptide tag and hydrophilic polystyrene plate
    • Y. Kumada, C. Zhao, R. Ishimura, H. Imanaka, K. Imamura, and K. Nakanishi Protein-protein interaction analysis using an affinity peptide tag and hydrophilic polystyrene plate J. Biotechnol. 128 2007 354 361
    • (2007) J. Biotechnol. , vol.128 , pp. 354-361
    • Kumada, Y.1    Zhao, C.2    Ishimura, R.3    Imanaka, H.4    Imamura, K.5    Nakanishi, K.6
  • 97
    • 77957311428 scopus 로고    scopus 로고
    • Efficient production of an antibody Fab fragment using the baculovirus-insect cell system
    • T. Furuta, T. Ogawa, T. Katsuda, I. Fujii, and H. Yamaji Efficient production of an antibody Fab fragment using the baculovirus-insect cell system J. Biosci. Bioeng. 110 2010 577 581
    • (2010) J. Biosci. Bioeng. , vol.110 , pp. 577-581
    • Furuta, T.1    Ogawa, T.2    Katsuda, T.3    Fujii, I.4    Yamaji, H.5
  • 98
    • 84867812849 scopus 로고    scopus 로고
    • Production of antibody fragments using the baculovirus-insect cell system
    • T. Furuta, T. Ogawa, and H. Yamaji Production of antibody fragments using the baculovirus-insect cell system Methods Mol. Biol. 907 2012 371 387
    • (2012) Methods Mol. Biol. , vol.907 , pp. 371-387
    • Furuta, T.1    Ogawa, T.2    Yamaji, H.3
  • 100
    • 0035166478 scopus 로고    scopus 로고
    • Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments
    • M. Liang, S. Dubel, D. Li, I. Queitsch, W. Li, and E.K. Bautz Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments J. Immunol. Methods 247 2001 119 130
    • (2001) J. Immunol. Methods , vol.247 , pp. 119-130
    • Liang, M.1    Dubel, S.2    Li, D.3    Queitsch, I.4    Li, W.5    Bautz, E.K.6
  • 101
    • 0030731752 scopus 로고    scopus 로고
    • Optimization of scFv antibody production in transgenic plants
    • U. Fiedler, J. Phillips, O. Artsaenko, and U. Conrad Optimization of scFv antibody production in transgenic plants Immunotechnology 3 1997 205 216
    • (1997) Immunotechnology , vol.3 , pp. 205-216
    • Fiedler, U.1    Phillips, J.2    Artsaenko, O.3    Conrad, U.4
  • 102
    • 84882972792 scopus 로고    scopus 로고
    • Generation and expression in plants of a single-chain variable fragment antibody against the immunodominant membrane protein of Candidatus phytoplasma aurantifolia
    • F. Shahryari, M.R. Safarnejad, M. Shams-Bakhsh, S. Schillberg, and G. Nolke Generation and expression in plants of a single-chain variable fragment antibody against the immunodominant membrane protein of Candidatus phytoplasma aurantifolia J. Microbiol. Biotechnol. 23 2013 1047 1054
    • (2013) J. Microbiol. Biotechnol. , vol.23 , pp. 1047-1054
    • Shahryari, F.1    Safarnejad, M.R.2    Shams-Bakhsh, M.3    Schillberg, S.4    Nolke, G.5
  • 103
    • 63949085617 scopus 로고    scopus 로고
    • Expression of anti-K99 scFv in transgenic rice tissues and its functional characterization
    • G. Sunilkumar, S.D. Waghela, L.M. Campbell, and K.S. Rathore Expression of anti-K99 scFv in transgenic rice tissues and its functional characterization Transgenic Res. 18 2009 347 360
    • (2009) Transgenic Res. , vol.18 , pp. 347-360
    • Sunilkumar, G.1    Waghela, S.D.2    Campbell, L.M.3    Rathore, K.S.4
  • 105
    • 70349615664 scopus 로고    scopus 로고
    • Direct immobilization of functional single-chain variable fragment antibodies (scFvs) onto a polystyrene plate by genetic fusion of a polystyrene-binding peptide (PS-tag)
    • Y. Kumada, K. Hamasaki, Y. Shiritani, A. Nakagawa, D. Kuroki, T. Ohse, D.H. Choi, Y. Katakura, and M. Kishimoto Direct immobilization of functional single-chain variable fragment antibodies (scFvs) onto a polystyrene plate by genetic fusion of a polystyrene-binding peptide (PS-tag) Anal. Bioanal. Chem. 395 2009 759 765
    • (2009) Anal. Bioanal. Chem. , vol.395 , pp. 759-765
    • Kumada, Y.1    Hamasaki, K.2    Shiritani, Y.3    Nakagawa, A.4    Kuroki, D.5    Ohse, T.6    Choi, D.H.7    Katakura, Y.8    Kishimoto, M.9
  • 106
    • 84866487628 scopus 로고    scopus 로고
    • Improved lectin ELISA for glycosylation analysis of biomarkers using PS-tag-fused single-chain Fv
    • Y. Kumada, Y. Ohigashi, Y. Emori, K. Imamura, Y. Omura, and M. Kishimoto Improved lectin ELISA for glycosylation analysis of biomarkers using PS-tag-fused single-chain Fv J. Immunol. Methods 385 2012 15 22
    • (2012) J. Immunol. Methods , vol.385 , pp. 15-22
    • Kumada, Y.1    Ohigashi, Y.2    Emori, Y.3    Imamura, K.4    Omura, Y.5    Kishimoto, M.6
  • 108
    • 84907052508 scopus 로고    scopus 로고
    • Efficient refolding and immobilization of PMMA-tag-fused single-chain Fv antibodies for sensitive immunological detection on a PMMA plate
    • (in press)
    • Y. Kumada, Y. Ishikawa, Y. Fujiwara, R. Takeda, R. Miyamoto, D. Niwa, S. Momose, B. Kang, and M. Kishimoto Efficient refolding and immobilization of PMMA-tag-fused single-chain Fv antibodies for sensitive immunological detection on a PMMA plate J. Immunol. Methods 2014 10.1016/j.jim.2014.05.015 (in press)
    • (2014) J. Immunol. Methods
    • Kumada, Y.1    Ishikawa, Y.2    Fujiwara, Y.3    Takeda, R.4    Miyamoto, R.5    Niwa, D.6    Momose, S.7    Kang, B.8    Kishimoto, M.9


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