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Volumn 420, Issue 1, 2012, Pages 54-60

Premature antibodies with rapid reaction kinetics and their characterization for diagnostic applications

Author keywords

Antibody binding kinetics; Binding kinetic transition; Continuous monitoring of myoglobin in serum; Immunization number of animal; Label free sensor

Indexed keywords

ANIMALS; ASSOCIATION REACTIONS; DISSOCIATION; IMMUNIZATION; KINETICS; RATE CONSTANTS;

EID: 80054916750     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.09.006     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0026345967 scopus 로고
    • Low affinity interaction of peptide-MHC complexes with T cell receptors
    • K. Matsui, J.J. Boniface, P.A. Reay, H. Schild, B. Fazekas de St Groth, and M.M. Davis Low affinity interaction of peptide-MHC complexes with T cell receptors Science 254 1991 1788 1791 (Pubitemid 21917527)
    • (1991) Science , vol.254 , Issue.5039 , pp. 1788-1791
    • Matsui, K.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Fazekas De St Groth, B.5    Davis, M.M.6
  • 2
    • 0027977974 scopus 로고
    • Transient intercellular adhesion: The importance of weak protein-protein interactions
    • DOI 10.1016/0968-0004(94)90109-0
    • P.A. van der Merwe, and A.N. Barclay Transient intercellular adhesion: the importance of weak protein-protein interactions Trends Biochem. Sci. 19 1994 354 358 (Pubitemid 24281499)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.9 , pp. 354-358
    • Van Der Merwe, P.A.1    Barclay, A.N.2
  • 4
    • 0033976397 scopus 로고    scopus 로고
    • Continuous weak-affinity immunosensing
    • DOI 10.1016/S0167-7799(99)01411-0, PII S0167779999014110
    • S. Ohlson, C. Jungar, M. Strandh, and C.F. Mandenius Continuous weak-affinity immunosensing Trends Biotechnol. 18 2000 49 52 (Pubitemid 30084695)
    • (2000) Trends in Biotechnology , vol.18 , Issue.2 , pp. 49-52
    • Ohlson, S.1    Jungar, C.2    Strandh, M.3    Mandenius, C.-F.4
  • 5
    • 0034214013 scopus 로고    scopus 로고
    • Analysis of carbohydrates using liquid chromatography-surface plasmon resonance immunosensing systems
    • DOI 10.1006/abio.2000.4565
    • C. Jungar, M. Strandh, S. Ohlson, and C.F. Mandenius Analysis of carbohydrates using liquid chromatography-surface plasmon resonance immunosensing systems Anal. Biochem. 281 2000 151 158 (Pubitemid 30346493)
    • (2000) Analytical Biochemistry , vol.281 , Issue.2 , pp. 151-158
    • Jungar, C.1    Strandh, M.2    Ohlson, S.3    Mandenius, C.-F.4
  • 6
    • 1842841979 scopus 로고    scopus 로고
    • Determination of kinetic data using surface plasmon resonance biosensors
    • C. Hahnefeld, S. Drewianka, and F.W. Herberg Determination of kinetic data using surface plasmon resonance biosensors Methods Mol. Med. 94 2004 299 320
    • (2004) Methods Mol. Med. , vol.94 , pp. 299-320
    • Hahnefeld, C.1    Drewianka, S.2    Herberg, F.W.3
  • 7
    • 0020692169 scopus 로고
    • Development of sensitive immunoassays for detection of antibodies against hepatitis B surface antigen
    • DOI 10.1016/0166-0934(83)90066-6
    • I. Ionescu-Matiu, Y. Sanchez, H.A. Fields, and G.R. Dreesman Development of sensitive immunoassays for detection of antibodies against hepatitis B surface antigen J. Virol. Methods 6 1983 41 52 (Pubitemid 13190977)
    • (1983) Journal of Virological Methods , vol.6 , Issue.1 , pp. 41-52
    • Ionescu Matiu, I.1    Sanchez, Y.2    Fields, H.A.3    Dreesman, G.R.4
  • 8
    • 1842373834 scopus 로고    scopus 로고
    • Performance characteristics of a reversible immunosensor with a heterobifunctional enzyme conjugate as signal generator
    • DOI 10.1002/(SICI)1097-0290(19971020)56:2<221::AID-BIT11>3.0.CO;2-J
    • S.H. Paek, and W. Schramm Performance characteristics of a reversible immunosensor with a heterobifunctional enzyme conjugate as signal generator Biotechnol. Bioeng. 56 1997 221 231 (Pubitemid 27430900)
    • (1997) Biotechnology and Bioengineering , vol.56 , Issue.2 , pp. 221-231
    • Paek, S.-H.1    Schramm, W.2
  • 10
    • 0025856601 scopus 로고
    • Kinetic maturation of an immune response
    • J. Foote, and C. Milstein Kinetic maturation of an immune response Nature 352 1991 530 532 (Pubitemid 21912377)
    • (1991) Nature , vol.352 , Issue.6335 , pp. 530-532
    • Foote, J.1    Milstein, C.2
  • 11
    • 0032489836 scopus 로고    scopus 로고
    • Diagnostic strategies using myoglobin measurement in myocardial infarction
    • DOI 10.1016/S0009-8981(97)00253-2, PII S0009898197002532
    • M. Plebani, and M. Zaninotto Diagnostic strategies using myoglobin measurement in myocardial infarction Clin. Chim. Acta 272 1998 69 77 (Pubitemid 28179618)
    • (1998) Clinica Chimica Acta , vol.272 , Issue.1 , pp. 69-77
    • Plebani, M.1    Zaninotto, M.2
  • 12
    • 0037373997 scopus 로고    scopus 로고
    • Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten
    • DOI 10.1016/S0161-5890(02)00282-1
    • T. Sagawa, M. Oda, M. Ishimura, K. Furukawa, and T. Azuma Thermodynamic and kinetic aspects of antibody evolution during the immune response to hapten Mol. Immunol. 39 2003 801 808 (Pubitemid 36263131)
    • (2003) Molecular Immunology , vol.39 , Issue.13 , pp. 801-808
    • Sagawa, T.1    Oda, M.2    Ishimura, M.3    Furukawa, K.4    Azuma, T.5
  • 13
    • 0018953062 scopus 로고
    • Production of monoclonal antibodies: Strategy and tactics
    • DOI 10.1016/0022-1759(80)90146-5
    • S. Fazekas de St Groth, and D. Scheidegger Production of monoclonal antibodies: strategy and tactics J. Immunol. Methods 35 1980 1 21 (Pubitemid 10034772)
    • (1980) Journal of Immunological Methods , vol.35 , Issue.1-2 , pp. 1-21
    • Fazekas De St.Groth, S.1    Scheidegger, D.2
  • 14
    • 0027328024 scopus 로고
    • Hybrid hybridomas producing bispecific antibodies to CEA and peroxidase isolated by a combination of HAT medium selection and fluorescence activated cell sorting
    • P. Jantscheff, L. Winkler, L. Karawajew, G. Kaiser, V. Bottger, and B. Micheel Hybrid hybridomas producing bispecific antibodies to CEA and peroxidase isolated by a combination of HAT medium selection and fluorescence activated cell sorting J. Immunol. Methods 163 1993 91 97
    • (1993) J. Immunol. Methods , vol.163 , pp. 91-97
    • Jantscheff, P.1    Winkler, L.2    Karawajew, L.3    Kaiser, G.4    Bottger, V.5    Micheel, B.6
  • 15
    • 0023186039 scopus 로고
    • Alternatives to pristane priming for ascitic fluid and monoclonal antibody production
    • DOI 10.1016/0022-1759(87)90027-5
    • R.W. Gillette Alternatives to pristane priming for ascitic fluid and monoclonal antibody production J. Immunol. Methods 99 1987 21 23 (Pubitemid 17089970)
    • (1987) Journal of Immunological Methods , vol.99 , Issue.1 , pp. 21-23
    • Gillette, R.W.1
  • 16
    • 21044449763 scopus 로고    scopus 로고
    • Industrial implementation of in vitro production of monoclonal antibodies
    • V. Dewar, P. Voet, F. Denamur, and J. Smal Industrial implementation of in vitro production of monoclonal antibodies ILAR J. 46 2005 307 313 (Pubitemid 40872938)
    • (2005) ILAR Journal , vol.46 , Issue.3 , pp. 307-313
    • Dewar, V.1    Voet, P.2    Denamur, F.3    Smal, J.4
  • 17
    • 32444437405 scopus 로고    scopus 로고
    • Plastic ELISA-on-a-chip based on sequential cross-flow chromatography
    • J.H. Cho, S.M. Han, E.H. Paek, I.H. Cho, and S.H. Paek Plastic ELISA-on-a-chip based on sequential cross-flow chromatography Anal. Chem. 78 2006 793 800
    • (2006) Anal. Chem. , vol.78 , pp. 793-800
    • Cho, J.H.1    Han, S.M.2    Paek, E.H.3    Cho, I.H.4    Paek, S.H.5
  • 18
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: A threshold, a ceiling, and the importance of off-rate
    • DOI 10.1016/S1074-7613(00)80580-4
    • F.D. Batista, and M.S. Neuberger Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate Immunity 8 1998 751 759 (Pubitemid 28294522)
    • (1998) Immunity , vol.8 , Issue.6 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 19
    • 0030026711 scopus 로고    scopus 로고
    • Affinity maturation and hypermutation in a simulation of the humoral immune response
    • DOI 10.1002/eji.1830260626
    • F. Celada, and P.E. Seiden Affinity maturation and hypermutation in a simulation of the humoral immune response Eur. J. Immunol. 26 1996 1350 1358 (Pubitemid 26001072)
    • (1996) European Journal of Immunology , vol.26 , Issue.6 , pp. 1350-1358
    • Celada, F.1    Seiden, P.E.2
  • 20
    • 43049120226 scopus 로고    scopus 로고
    • Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    • Y. Abdiche, D. Malashock, A. Pinkerton, and J. Pons Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet Anal. Biochem. 377 2008 209 217
    • (2008) Anal. Biochem. , vol.377 , pp. 209-217
    • Abdiche, Y.1    Malashock, D.2    Pinkerton, A.3    Pons, J.4
  • 21
    • 79952613759 scopus 로고    scopus 로고
    • Minimum-step immuno-analysis based on continuous recycling of the capture antibody
    • H.K. Cho, S.M. Seo, I.H. Cho, S.H. Paek, D.H. Kim, and S.H. Paek Minimum-step immuno-analysis based on continuous recycling of the capture antibody Analyst 136 2011 1374 1379
    • (2011) Analyst , vol.136 , pp. 1374-1379
    • Cho, H.K.1    Seo, S.M.2    Cho, I.H.3    Paek, S.H.4    Kim, D.H.5    Paek, S.H.6
  • 22
    • 0027745741 scopus 로고
    • Noninvasive assessment of reperfusion and reocclusion after thrombolysis in acute myocardial infarction
    • P. Klootwijk, C. Cobbaert, P. Fioretti, P.P. Kint, and M.L. Simoons Noninvasive assessment of reperfusion and reocclusion after thrombolysis in acute myocardial infarction Am. J. Cardiol. 72 1993 75G 84G (Pubitemid 24023490)
    • (1993) American Journal of Cardiology , vol.72 , Issue.19
    • Klootwijk, P.1    Cobbaert, C.2    Fioretti, P.3    Kint, P.P.4    Simoons, M.L.5
  • 24
    • 0035095162 scopus 로고    scopus 로고
    • (Immuno)affinity chromatography: A versatile tool for fast and selective purification, concentration, isolation and analysis
    • DOI 10.1016/S0731-7085(00)00549-5, PII S0731708500005495
    • M.M. Rhemrev-Boom, M. Yates, M. Rudolph, and M. Raedts (Immuno)affinity chromatography: a versatile tool for fast and selective purification, concentration, isolation, and analysis J. Pharm. Biomed. Anal. 24 2001 825 833 (Pubitemid 32209138)
    • (2001) Journal of Pharmaceutical and Biomedical Analysis , vol.24 , Issue.5-6 , pp. 825-833
    • Rhemrev-Boom, M.M.1    Yates, M.2    Rudolph, M.3    Raedts, M.4
  • 25
    • 0037204853 scopus 로고    scopus 로고
    • Purification of antibodies by affinity chromatography
    • DOI 10.1016/S0165-022X(02)00017-9, PII S0165022X02000179
    • K. Huse, H.J. Bohme, and G.H. Scholz Purification of antibodies by affinity chromatography J. Biochem. Biophys. Methods 51 2002 217 231 (Pubitemid 34671136)
    • (2002) Journal of Biochemical and Biophysical Methods , vol.51 , Issue.3 , pp. 217-231
    • Huse, K.1    Bohme, H.-J.2    Scholz, G.H.3
  • 26
    • 0024593180 scopus 로고
    • Epitope model of tick-borne encephalitis virus envelope glycoprotein E: Analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH
    • DOI 10.1016/0042-6822(89)90044-5
    • F. Guirakhoo, F.X. Heinz, and C. Kunz Epitope model of tick-borne encephalitis virus envelope glycoprotein E: analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH Virology 169 1989 90 99 (Pubitemid 19080151)
    • (1989) Virology , vol.169 , Issue.1 , pp. 90-99
    • Guirakhoo, F.1    Heinz, F.X.2    Kunz, C.3
  • 27
  • 28
    • 0032940238 scopus 로고    scopus 로고
    • Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
    • DOI 10.1016/S0167-4838(99)00046-1, PII S0167483899000461
    • K. Wel£e, R. Misselwitz, G. Hausdorf, W. Hohne, and H. Wel£e Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments Biochim. Biophys. Acta 1431 1999 120 131 (Pubitemid 29182728)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1431 , Issue.1 , pp. 120-131
    • Welfle, K.1    Misselwitz, R.2    Hausdorf, G.3    Hohne, W.4    Welfle, H.5
  • 29
    • 33847059215 scopus 로고    scopus 로고
    • Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
    • D. Ejima, K. Tsumoto, H. Fukada, R. Yumioka, K. Nagase, T. Arakawa, and J.S. Philo Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies Proteins 66 2007 954 962
    • (2007) Proteins , vol.66 , pp. 954-962
    • Ejima, D.1    Tsumoto, K.2    Fukada, H.3    Yumioka, R.4    Nagase, K.5    Arakawa, T.6    Philo, J.S.7
  • 30
    • 0032518373 scopus 로고    scopus 로고
    • Structural basis of pH-dependent antibody binding by the neonatal Fc receptor
    • D.E. Vaughn, and P.J. Bjorkman Structural basis of pH-dependent antibody binding by the neonatal Fc receptor Structure 6 1998 63 73 (Pubitemid 28084400)
    • (1998) Structure , vol.6 , Issue.1 , pp. 63-73
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 31
    • 33747830523 scopus 로고    scopus 로고
    • Additive assay of cancer marker CA 19-9 by SPR biosensor
    • DOI 10.1016/j.snb.2006.04.015, PII S0925400506002632
    • J.W. Chung, R. Bernhardt, and J.C. Pyun Additive assay of cancer marker CA 19-9 by SPR biosensor Sens. Actuators B 118 2006 28 32 (Pubitemid 44287386)
    • (2006) Sensors and Actuators, B: Chemical , vol.118 , Issue.1-2 , pp. 28-32
    • Chung, J.W.1    Bernhardt, R.2    Pyun, J.C.3
  • 32
    • 0024506474 scopus 로고
    • Improved competitive enzyme-linked immunoassay (ELISA) for albuminuria
    • R.G. Neuman, and M.P. Cohen Improved competitive enzyme-linked immunoassay (ELISA) for albuminuria Clin. Chim. Acta 179 1989 229 237
    • (1989) Clin. Chim. Acta , vol.179 , pp. 229-237
    • Neuman, R.G.1    Cohen, M.P.2
  • 33
    • 0033401013 scopus 로고    scopus 로고
    • Enzyme-linked competitive binding assay based on the biotin/avidin interaction
    • H.C. Cho, D.J. Lee, S.Y. Kim, J.H. Kim, I.R. Paeng, and G.S. Cha Enzyme-linked competitive binding assay based on the biotin/avidin interaction Anal. Sci. 15 1999 343 347
    • (1999) Anal. Sci. , vol.15 , pp. 343-347
    • Cho, H.C.1    Lee, D.J.2    Kim, S.Y.3    Kim, J.H.4    Paeng, I.R.5    Cha, G.S.6
  • 35
    • 74549172591 scopus 로고    scopus 로고
    • The utilization of BSA-modified chip on the investigation of ligand/protein interaction with surface plasma resonance
    • L. Chen, Q. Wang, and W. Hou The utilization of BSA-modified chip on the investigation of ligand/protein interaction with surface plasma resonance Afr. J. Biotechnol. 8 2009 7148 7155
    • (2009) Afr. J. Biotechnol. , vol.8 , pp. 7148-7155
    • Chen, L.1    Wang, Q.2    Hou, W.3


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