메뉴 건너뛰기




Volumn 437, Issue 2, 2013, Pages 118-122

Nanomolar to sub-picomolar affinity measurements of antibody-antigen interactions and protein multimerizations: Fluorescence-assisted high-performance liquid chromatography

Author keywords

Binding assay; Dissociation constant; High affinity; High performance liquid chromatography

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; ANTIGENS; DISSOCIATION; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MONOCLONAL ANTIBODIES; SURFACE PLASMON RESONANCE;

EID: 84875983163     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.02.027     Document Type: Article
Times cited : (10)

References (17)
  • 4
    • 33746742909 scopus 로고    scopus 로고
    • Looking towards label-free biomolecular interaction analysis in a high-throughput format: A review of new surface plasmon resonance technologies
    • DOI 10.1016/j.copbio.2006.06.012, PII S0958166906000966
    • C. Boozer, G. Kim, S. Cong, H. Guan, and T. Londergan Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies Curr. Opin. Biotechnol. 17 2006 400 405 (Pubitemid 44163461)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 400-405
    • Boozer, C.1    Kim, G.2    Cong, S.3    Guan, H.4    Londergan, T.5
  • 5
    • 79551605802 scopus 로고    scopus 로고
    • Label-free assessment of high-affinity antibody-antigen binding constants: Comparison of bioassay, SPR, and PEIA-ellipsometry
    • T. Rispens, V.H. Te, P. Hemker, H. Speijer, W. Hermens, and L. Aarden Label-free assessment of high-affinity antibody-antigen binding constants: comparison of bioassay, SPR, and PEIA-ellipsometry J. Immunol. Methods 365 2011 50 57
    • (2011) J. Immunol. Methods , vol.365 , pp. 50-57
    • Rispens, T.1    Te, V.H.2    Hemker, P.3    Speijer, H.4    Hermens, W.5    Aarden, L.6
  • 6
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods
    • DOI 10.1016/j.ab.2003.12.025, PII S0003269704000673
    • A.W. Drake, D.G. Myszka, and S.L. Klakamp Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods Anal. Biochem. 328 2004 35 43 (Pubitemid 38479615)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 35-43
    • Drake, A.W.1    Myszka, D.G.2    Klakamp, S.L.3
  • 7
    • 27744566590 scopus 로고    scopus 로고
    • Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection
    • DOI 10.1016/j.ab.2005.09.007, PII S0003269705006718
    • K. High, Y. Meng, M.W. Washabaugh, and Q. Zhao Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection Anal. Biochem. 347 2005 159 161 (Pubitemid 41608581)
    • (2005) Analytical Biochemistry , vol.347 , Issue.1 , pp. 159-161
    • High, K.1    Meng, Y.2    Washabaugh, M.W.3    Zhao, Q.4
  • 8
    • 0031027480 scopus 로고    scopus 로고
    • Assessment of affinity constants by rapid solid phase detection of equilibrium binding in a flow system
    • DOI 10.1016/S0022-1759(96)00222-0, PII S0022175996002220
    • J. Piehler, A. Brecht, T. Giersch, B. Hock, and G. Gauglitz Assessment of affinity constants by rapid solid phase detection of equilibrium binding in a flow system J. Immunol. Methods 201 1997 189 206 (Pubitemid 27086716)
    • (1997) Journal of Immunological Methods , vol.201 , Issue.2 , pp. 189-206
    • Piehler, J.1    Brecht, A.2    Giersch, T.3    Hock, B.4    Gauglitz, G.5
  • 9
    • 84858273630 scopus 로고    scopus 로고
    • Characterization of neutralizing affinity-matured human respiratory syncytial virus F binding antibodies in the sub-picomolar affinity range
    • G.A. Canziani, J.A. Melero, and E.R. Lacy Characterization of neutralizing affinity-matured human respiratory syncytial virus F binding antibodies in the sub-picomolar affinity range J. Mol. Recognit. 25 2012 136 146
    • (2012) J. Mol. Recognit. , vol.25 , pp. 136-146
    • Canziani, G.A.1    Melero, J.A.2    Lacy, E.R.3
  • 10
    • 63749093322 scopus 로고    scopus 로고
    • Comparisons of affinities, avidities, and complement activation of adalimumab, infliximab, and etanercept in binding to soluble and membrane tumor necrosis factor
    • Z. Kaymakcalan, P. Sakorafas, S. Bose, S. Scesney, L. Xiong, D.K. Hanzatian, J. Salfeld, and E.H. Sasso Comparisons of affinities, avidities, and complement activation of adalimumab, infliximab, and etanercept in binding to soluble and membrane tumor necrosis factor Clin. Immunol. 131 2009 308 316
    • (2009) Clin. Immunol. , vol.131 , pp. 308-316
    • Kaymakcalan, Z.1    Sakorafas, P.2    Bose, S.3    Scesney, S.4    Xiong, L.5    Hanzatian, D.K.6    Salfeld, J.7    Sasso, E.H.8
  • 11
    • 23044494423 scopus 로고    scopus 로고
    • Demonstration of an in vivo generated sub-picomolar affinity fully human monoclonal antibody to interleukin-8
    • DOI 10.1016/j.bbrc.2005.07.002, PII S0006291X05014452
    • P. Rathanaswami, S. Roalstad, L. Roskos, Q.J. Su, S. Lackie, and J. Babcook Demonstration of an in vivo generated sub-picomolar affinity fully human monoclonal antibody to interleukin-8 Biochem. Biophys. Res. Commun. 334 2005 1004 1013 (Pubitemid 41074676)
    • (2005) Biochemical and Biophysical Research Communications , vol.334 , Issue.4 , pp. 1004-1013
    • Rathanaswami, P.1    Roalstad, S.2    Roskos, L.3    Su, Q.J.4    Lackie, S.5    Babcook, J.6
  • 14
    • 0031016202 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium of uncomplemented M15 β-galactosidase from Escherichia coli
    • DOI 10.1021/bi961347a
    • C.N. Gallagher, and R.E. Huber Monomer-dimer equilibrium of uncomplemented M15 β-galactosidase from Escherichia coli Biochemistry 36 1997 1281 1286 (Pubitemid 27074951)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1281-1286
    • Gallagher, C.N.1    Huber, R.E.2
  • 15
    • 0033829953 scopus 로고    scopus 로고
    • From gel filtration to biosensor technology: The development of chromatography for the characterization of protein interactions
    • D.J. Winzor From gel filtration to biosensor technology: the development of chromatography for the characterization of protein interactions J. Mol. Recognit. 13 2000 279 298
    • (2000) J. Mol. Recognit. , vol.13 , pp. 279-298
    • Winzor, D.J.1
  • 16
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • J. Foote, and H.N. Eisen Kinetic and affinity limits on antibodies produced during immune responses Proc. Natl. Acad. Sci. USA 92 1995 1254 1256
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 17
    • 0034718592 scopus 로고    scopus 로고
    • Breaking the affinity ceiling for antibodies and T cell receptors
    • J. Foote, and H.N. Eisen Breaking the affinity ceiling for antibodies and T cell receptors Proc. Natl. Acad. Sci. USA 97 2000 10679 10681
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10679-10681
    • Foote, J.1    Eisen, H.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.