메뉴 건너뛰기




Volumn 280, Issue 1-2, 2003, Pages 183-1202

Kinetic analysis of interactions between bispecific monoclonal antibodies and immobilized antigens using a resonant mirror biosensor

Author keywords

Bispecific antibodies; Bivalent interaction; IAsys; Kinetic constants; Resonant mirror biosensor

Indexed keywords

ANTIGEN; HORSERADISH PEROXIDASE; MONOCLONAL ANTIBODY;

EID: 0142075299     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(03)00271-0     Document Type: Article
Times cited : (29)

References (49)
  • 3
    • 0032212020 scopus 로고    scopus 로고
    • Bispecific antibodies as novel bioconjugates
    • Cao Y., Suresh M.R. Bispecific antibodies as novel bioconjugates. Bioconjug. Chem. 9:1998;635.
    • (1998) Bioconjug. Chem. , vol.9 , pp. 635
    • Cao, Y.1    Suresh, M.R.2
  • 4
    • 0031059402 scopus 로고    scopus 로고
    • Design and production of novel tetravalent bispecific antibodies
    • Coloma M.J., Morrison S.L. Design and production of novel tetravalent bispecific antibodies. Nat. Biotechnol. 15:1997;159.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 159
    • Coloma, M.J.1    Morrison, S.L.2
  • 5
    • 0015313012 scopus 로고
    • The influence of polyvalency on binding properties of antibodies
    • Crothers D.M., Metzger H. The influence of polyvalency on binding properties of antibodies. Immunochemistry. 9:1972;341.
    • (1972) Immunochemistry , vol.9 , pp. 341
    • Crothers, D.M.1    Metzger, H.2
  • 6
    • 0027366806 scopus 로고
    • The resonant mirror: A novel optical biosensor for direct sensing of biomolecular interactions: Part I. Principle of operation and associated instrumentation
    • Cush R., Cronin J.M., Stewart W.J., Maule C.H., Molloy J., Goddard N.J. The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions: Part I. Principle of operation and associated instrumentation. Biosens. Bioelectron. 8:1993;347.
    • (1993) Biosens. Bioelectron. , vol.8 , pp. 347
    • Cush, R.1    Cronin, J.M.2    Stewart, W.J.3    Maule, C.H.4    Molloy, J.5    Goddard, N.J.6
  • 8
    • 0032190570 scopus 로고    scopus 로고
    • Determination of CD4 antigen density on cells: Role of antibody valency, avidity, clones, and conjugation
    • Davis K.A., Abrams B., Iyer S.B., Hoffman R.A., Bishop J.E. Determination of CD4 antigen density on cells: role of antibody valency, avidity, clones, and conjugation. Cytometry. 33:1998;197.
    • (1998) Cytometry , vol.33 , pp. 197
    • Davis, K.A.1    Abrams, B.2    Iyer, S.B.3    Hoffman, R.A.4    Bishop, J.E.5
  • 9
    • 0003538021 scopus 로고
    • The specificity of monoclonal antibodies for enzymes in solution vs. immobilized on solid phase
    • J.E. Butler. Boca Raton, FL: CRC Press
    • Djavadi-Ohaniance L., Friguet B. The specificity of monoclonal antibodies for enzymes in solution vs. immobilized on solid phase. Butler J.E. The Immunochemistry of Solid-Phase Immunoassay. 1991;199 CRC Press, Boca Raton, FL.
    • (1991) The Immunochemistry of Solid-Phase Immunoassay , pp. 199
    • Djavadi-Ohaniance, L.1    Friguet, B.2
  • 10
    • 0034988033 scopus 로고    scopus 로고
    • The comparison of the ability of monoclonal antibodies directed to different proteins (human IgG, human myoglobin and HRP) and bispecific antibodies derived thereof to bind antigens immobilized on a surface of a solid phase
    • Dmitriev D.A., Massino Y.S., Segal O.L., Smirnova M.B., Kolyaskina G.I., Pavlova E.V., Osipov A.P., Egorov A.M., Dmitriev A.D. The comparison of the ability of monoclonal antibodies directed to different proteins (human IgG, human myoglobin and HRP) and bispecific antibodies derived thereof to bind antigens immobilized on a surface of a solid phase. Clin. Chim. Acta. 309:2001;57.
    • (2001) Clin. Chim. Acta , vol.309 , pp. 57
    • Dmitriev, D.A.1    Massino, Y.S.2    Segal, O.L.3    Smirnova, M.B.4    Kolyaskina, G.I.5    Pavlova, E.V.6    Osipov, A.P.7    Egorov, A.M.8    Dmitriev, A.D.9
  • 12
    • 0021352499 scopus 로고
    • The interaction of monoclonal antibodies with MHC class I antigens on mouse spleen cells: I. Analysis of the mechanism of binding
    • Dower S.K., Ozato K., Segal D.M. The interaction of monoclonal antibodies with MHC class I antigens on mouse spleen cells: I. Analysis of the mechanism of binding. J. Immunol. 132:1984;751.
    • (1984) J. Immunol. , vol.132 , pp. 751
    • Dower, S.K.1    Ozato, K.2    Segal, D.M.3
  • 14
    • 0032189909 scopus 로고    scopus 로고
    • Second-order kinetic analysis of IAsys biosensor data: Its use and applicability
    • Edwards P.R., Maule C.H., Leatherbarrow R.J., Winzor D.J. Second-order kinetic analysis of IAsys biosensor data: its use and applicability. Anal. Biochem. 263:1998;1.
    • (1998) Anal. Biochem. , vol.263 , pp. 1
    • Edwards, P.R.1    Maule, C.H.2    Leatherbarrow, R.J.3    Winzor, D.J.4
  • 16
    • 0029053975 scopus 로고
    • Measurement of kinetic binding constants of a panel of anti-saporin antibodies using a resonant mirror biosensor
    • George A.J.T., French R.R., Glennie M.J. Measurement of kinetic binding constants of a panel of anti-saporin antibodies using a resonant mirror biosensor. J. Immunol. Methods. 183:1995;51.
    • (1995) J. Immunol. Methods , vol.183 , pp. 51
    • George, A.J.T.1    French, R.R.2    Glennie, M.J.3
  • 17
    • 0030592117 scopus 로고    scopus 로고
    • Analysis of kinetic data of antibody-antigen interaction from an optical biosensor by exponential curve fitting
    • Gill A., Leatherbarrow R.J., Hoare M., Pollard-Knight D.V., Lowe P.A., Fortune D.H. Analysis of kinetic data of antibody-antigen interaction from an optical biosensor by exponential curve fitting. J. Biotechnol. 48:1996;117.
    • (1996) J. Biotechnol. , vol.48 , pp. 117
    • Gill, A.1    Leatherbarrow, R.J.2    Hoare, M.3    Pollard-Knight, D.V.4    Lowe, P.A.5    Fortune, D.H.6
  • 18
    • 0036132656 scopus 로고    scopus 로고
    • Direct kinetic assay of interactions between small peptides and immobilized antibodies using a surface plasmon resonance biosensor
    • Gomes P., Andreu D. Direct kinetic assay of interactions between small peptides and immobilized antibodies using a surface plasmon resonance biosensor. J. Immunol. Methods. 259:2002;217.
    • (2002) J. Immunol. Methods , vol.259 , pp. 217
    • Gomes, P.1    Andreu, D.2
  • 19
    • 0031034811 scopus 로고    scopus 로고
    • Use of a resonant mirror biosensor to characterize the interaction of carboxypeptidase A with an elicited monoclonal antibody
    • Hall D.R., Winzor D.J. Use of a resonant mirror biosensor to characterize the interaction of carboxypeptidase A with an elicited monoclonal antibody. Anal. Biochem. 244:1997;152.
    • (1997) Anal. Biochem. , vol.244 , pp. 152
    • Hall, D.R.1    Winzor, D.J.2
  • 20
    • 0031573450 scopus 로고    scopus 로고
    • Theoretical and experimental considerations of the pseudo-first-order approximation in conventional kinetic analysis of IAsys biosensor date
    • Hall D.R., Gorgani N.N., Altin J.G., Winzor D.J. Theoretical and experimental considerations of the pseudo-first-order approximation in conventional kinetic analysis of IAsys biosensor date. Anal. Biochem. 253:1997;145.
    • (1997) Anal. Biochem. , vol.253 , pp. 145
    • Hall, D.R.1    Gorgani, N.N.2    Altin, J.G.3    Winzor, D.J.4
  • 21
    • 0028710393 scopus 로고
    • Biosensor analysis of antigen-antibody interactions as a priority step in the generation of monoclonal bispecific antibodies
    • Horenstein A., Poiesi C., Camagna M., de Monte L., Mariani M., Albertini A., Malavasi F. Biosensor analysis of antigen-antibody interactions as a priority step in the generation of monoclonal bispecific antibodies. Cell Biophys. 24-25:1994;109.
    • (1994) Cell Biophys. , vol.24-25 , pp. 109
    • Horenstein, A.1    Poiesi, C.2    Camagna, M.3    De Monte, L.4    Mariani, M.5    Albertini, A.6    Malavasi, F.7
  • 22
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson R., Michaelsson A., Mattsson L. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods. 145:1991;229.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 23
    • 0025094259 scopus 로고
    • Polyvalent interaction of antibodies with bacterial cells
    • Karulin A.Yu., Dzantiev B.B. Polyvalent interaction of antibodies with bacterial cells. Mol. Immunol. 27:1990;965.
    • (1990) Mol. Immunol. , vol.27 , pp. 965
    • Karulin, A.Yu.1    Dzantiev, B.B.2
  • 24
    • 0026705890 scopus 로고
    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays
    • Kaufman E.N., Jain R.K. Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays. Cancer Res. 52:1992;4157.
    • (1992) Cancer Res. , vol.52 , pp. 4157
    • Kaufman, E.N.1    Jain, R.K.2
  • 25
    • 0028957940 scopus 로고
    • Protection from lethal coronavirus infection by immunoglobulin fragments
    • Lamarre A., Talbot P.J. Protection from lethal coronavirus infection by immunoglobulin fragments. J. Immunol. 154:1995;3975.
    • (1995) J. Immunol. , vol.154 , pp. 3975
    • Lamarre, A.1    Talbot, P.J.2
  • 26
    • 0001377675 scopus 로고
    • Kinetics of antibody reactions and the analysis of cell surface antigens
    • D.M. Weir. Oxford: Blackwell
    • Mason D.W., Williams A.F. Kinetics of antibody reactions and the analysis of cell surface antigens. Weir D.M. Handbook of Experimental Immunology. 4th ed. 1980;38.1 Blackwell, Oxford.
    • (1980) Handbook of Experimental Immunology 4th ed. , pp. 381
    • Mason, D.W.1    Williams, A.F.2
  • 27
    • 0026655782 scopus 로고
    • Construction of a quadroma to α-endorphin/horseradish peroxidase using an actinomycin D-resistant mouse myeloma cell line
    • Massino Y.S., Kizim E.A., Dergunova N.N., Vostrikov V.M., Dmitriev A.D. Construction of a quadroma to α-endorphin/horseradish peroxidase using an actinomycin D-resistant mouse myeloma cell line. Immunol. Lett. 33:1992;217.
    • (1992) Immunol. Lett. , vol.33 , pp. 217
    • Massino, Y.S.1    Kizim, E.A.2    Dergunova, N.N.3    Vostrikov, V.M.4    Dmitriev, A.D.5
  • 30
    • 0028875269 scopus 로고
    • On the validity of "functional affinity" determination for antibodies binding to cell surface antigens or other polyvalent antigens
    • Mattes M.J. On the validity of "functional affinity" determination for antibodies binding to cell surface antigens or other polyvalent antigens. Cancer Res. 55:1995;5733.
    • (1995) Cancer Res. , vol.55 , pp. 5733
    • Mattes, M.J.1
  • 31
    • 0343052036 scopus 로고    scopus 로고
    • Binding parameters of antibodies reacting with multivalent antigens: Functional affinity or pseudo-affinity
    • Mattes M.J. Binding parameters of antibodies reacting with multivalent antigens: functional affinity or pseudo-affinity. J. Immunol. Methods. 202:1997;97.
    • (1997) J. Immunol. Methods , vol.202 , pp. 97
    • Mattes, M.J.1
  • 32
    • 0030757999 scopus 로고    scopus 로고
    • Correlation between the avidity of mouse-human chimeric IgG subclass monoclonal antibodies measured by solid-phase elution ELISA and biospecific interaction analysis (BIA)
    • McCloskey N., Turner M.W., Goldblatt D. Correlation between the avidity of mouse-human chimeric IgG subclass monoclonal antibodies measured by solid-phase elution ELISA and biospecific interaction analysis (BIA). J. Immunol. Methods. 205:1997;67.
    • (1997) J. Immunol. Methods , vol.205 , pp. 67
    • McCloskey, N.1    Turner, M.W.2    Goldblatt, D.3
  • 33
    • 0020518331 scopus 로고
    • Hybrid hybridomas and their use in immunohistochemistry
    • Milstein C., Cuello A.C. Hybrid hybridomas and their use in immunohistochemistry. Nature. 305:1983;537.
    • (1983) Nature , vol.305 , pp. 537
    • Milstein, C.1    Cuello, A.C.2
  • 34
    • 0000265925 scopus 로고
    • Hybrid hybridomas and the production of bispecific monoclonal antibodies
    • Milstein C., Cuello A.C. Hybrid hybridomas and the production of bispecific monoclonal antibodies. Immunol. Today. 5:1984;299.
    • (1984) Immunol. Today , vol.5 , pp. 299
    • Milstein, C.1    Cuello, A.C.2
  • 35
    • 0032144281 scopus 로고    scopus 로고
    • Model and simulation of multivalent binding to fixed ligands
    • Muller K.M., Arndt K.M., Pluckthun A. Model and simulation of multivalent binding to fixed ligands. Anal. Biochem. 261:1998;149.
    • (1998) Anal. Biochem. , vol.261 , pp. 149
    • Muller, K.M.1    Arndt, K.M.2    Pluckthun, A.3
  • 36
    • 0038867807 scopus 로고    scopus 로고
    • A dimeric bispecific miniantibody combines two specificities with avidity
    • Muller K.M., Arndt K.M., Pluckthun A. A dimeric bispecific miniantibody combines two specificities with avidity. FEBS Lett. 432:1998;45.
    • (1998) FEBS Lett. , vol.432 , pp. 45
    • Muller, K.M.1    Arndt, K.M.2    Pluckthun, A.3
  • 37
    • 0030152062 scopus 로고    scopus 로고
    • Analysis of the interaction between a synthetic peptide of influenza virus hemagglutinin and monoclonal antibodies using an optical biosensor
    • Nice E.C., McInerney T.L., Jackson D.C. Analysis of the interaction between a synthetic peptide of influenza virus hemagglutinin and monoclonal antibodies using an optical biosensor. Mol. Immunol. 33:1996;659.
    • (1996) Mol. Immunol. , vol.33 , pp. 659
    • Nice, E.C.1    McInerney, T.L.2    Jackson, D.C.3
  • 39
    • 0029939283 scopus 로고    scopus 로고
    • Interpretation of deviations from pseudo-first order kinetic behavior in the characterization of ligand binding by biosensor technology
    • O'Shannessy D.J., Winsor D.J. Interpretation of deviations from pseudo-first order kinetic behavior in the characterization of ligand binding by biosensor technology. Anal. Biochem. 236:1996;275.
    • (1996) Anal. Biochem. , vol.236 , pp. 275
    • O'Shannessy, D.J.1    Winsor, D.J.2
  • 40
    • 0027293351 scopus 로고
    • Determination of rate and equilibrium binding constants for macromolecular interaction using surface plasmon resonance: Use of nonlinear least squares analysis methods
    • O'Shannessy D.J., Brigham-Burke M., Soneson K.K., Hensley P., Brooks I. Determination of rate and equilibrium binding constants for macromolecular interaction using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212:1993;457.
    • (1993) Anal. Biochem. , vol.212 , pp. 457
    • O'Shannessy, D.J.1    Brigham-Burke, M.2    Soneson, K.K.3    Hensley, P.4    Brooks, I.5
  • 41
    • 0027422957 scopus 로고
    • Measurement of kinetic binding constants of viral antibodies using a new biosensor technology
    • Pellequer J.L., Van Regenmortel M.H. Measurement of kinetic binding constants of viral antibodies using a new biosensor technology. J. Immunol. Methods. 166:1993;133.
    • (1993) J. Immunol. Methods , vol.166 , pp. 133
    • Pellequer, J.L.1    Van Regenmortel, M.H.2
  • 42
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • Pluckthun A., Pack P. New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology. 3:1997;83.
    • (1997) Immunotechnology , vol.3 , pp. 83
    • Pluckthun, A.1    Pack, P.2
  • 43
    • 0028120417 scopus 로고
    • Real-time biospecific interaction analysis of a natural human polyreactive monoclonal IgM antibody and its Fab and scFv fragments with several antigens
    • Roggenbuck D., Konig H., Niemann B., Schoenherr G., Jahn S., Porstmann T. Real-time biospecific interaction analysis of a natural human polyreactive monoclonal IgM antibody and its Fab and scFv fragments with several antigens. Scand. J. Immunol. 40:1994;64.
    • (1994) Scand. J. Immunol. , vol.40 , pp. 64
    • Roggenbuck, D.1    Konig, H.2    Niemann, B.3    Schoenherr, G.4    Jahn, S.5    Porstmann, T.6
  • 44
    • 0028983571 scopus 로고
    • "Anticardiolipin" autoantibodies recognise beta 2-glycoprotein I in the absence of phospholipid. Importance of Ag density and bivalent binding
    • Roubey R.A., Eisenberg R.A., Harper M.F., Winfield J.B. "Anticardiolipin" autoantibodies recognise beta 2-glycoprotein I in the absence of phospholipid. Importance of Ag density and bivalent binding. J. Immunol. 154:1995;954.
    • (1995) J. Immunol. , vol.154 , pp. 954
    • Roubey, R.A.1    Eisenberg, R.A.2    Harper, M.F.3    Winfield, J.B.4
  • 45
    • 0030571002 scopus 로고    scopus 로고
    • Analysis of mass transport-limited binding kinetics in evanescent wave biosensors
    • Schuck P., Minton A.P. Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240:1996;262.
    • (1996) Anal. Biochem. , vol.240 , pp. 262
    • Schuck, P.1    Minton, A.P.2
  • 48
    • 0027405124 scopus 로고
    • Development of a bispecific monoclonal antibody against a gallium-67 chelate and the human melanoma-associated antigen p97 for potential use in pretargeted immunoscintigraphy
    • Somasundaram C., Matzku S., Schuhmacher J., Zoller M. Development of a bispecific monoclonal antibody against a gallium-67 chelate and the human melanoma-associated antigen p97 for potential use in pretargeted immunoscintigraphy. Cancer Immunol. Immunother. 36:1993;337.
    • (1993) Cancer Immunol. Immunother. , vol.36 , pp. 337
    • Somasundaram, C.1    Matzku, S.2    Schuhmacher, J.3    Zoller, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.