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Volumn 12, Issue 5, 1999, Pages 300-309

Active concentration measurements of recombinant biomolecules using biosensor technology

Author keywords

Antibody fragments; Binding activity; CD4; Concentration measurement; gp120; Recombinant proteins; Surface plasmon resonance

Indexed keywords

BIOSENSOR; RECOMBINANT DNA TECHNOLOGY;

EID: 0032722542     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199909/10)12:5<300::AID-JMR467>3.0.CO;2-N     Document Type: Article
Times cited : (35)

References (40)
  • 2
    • 0031816582 scopus 로고    scopus 로고
    • Biosensor characterization of antigenic site A of foot-and-mouth disease virus presented in different vector systems
    • Benito, A. and Van Regenmortel, M. H. V. (1998). Biosensor characterization of antigenic site A of foot-and-mouth disease virus presented in different vector systems. FEMS Immunol. Med. Microbiol. 21, 201-215.
    • (1998) FEMS Immunol. Med. Microbiol. , vol.21 , pp. 201-215
    • Benito, A.1    Van Regenmortel, M.H.V.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford1
  • 4
    • 0026768221 scopus 로고
    • Detection of receptor-ligand interactions using surface plasmon resonance: Model studies employing the HIV-1 gp120/CD4 interaction
    • Brigham-Burke, M., Edwards, J. R. and O'Shannessy, D. (1992). Detection of receptor-ligand interactions using surface plasmon resonance: model studies employing the HIV-1 gp120/CD4 Interaction. Anal. Biochem. 205, 125-131.
    • (1992) Anal. Biochem. , vol.205 , pp. 125-131
    • Brigham-Burke, M.1    Edwards, J.R.2    O'Shannessy, D.3
  • 7
    • 0023905451 scopus 로고
    • Monoclonal antibodies as probes of conformational changes in protein-engineered cytochrome C
    • Callawn, J. F., Wallace, C. J. A., Proudfoot, A. E. I. and Paterson, Y. (1988). Monoclonal antibodies as probes of conformational changes in protein-engineered cytochrome C. J. Biol. Chem. 263, 8625-8634.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8625-8634
    • Callawn, J.F.1    Wallace, C.J.A.2    Proudfoot, A.E.I.3    Paterson, Y.4
  • 8
    • 0033596904 scopus 로고    scopus 로고
    • Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein
    • Choulier, L., Rauffer-Bruyère, N., Ben Kalifa, M., Martin, F., Vernet, T. and Altschuh, D. (1999). Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein. Biochemistry 38, 3530-3537.
    • (1999) Biochemistry , vol.38 , pp. 3530-3537
    • Choulier, L.1    Rauffer-Bruyère, N.2    Ben Kalifa, M.3    Martin, F.4    Vernet, T.5    Altschuh, D.6
  • 9
    • 0031194188 scopus 로고    scopus 로고
    • Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation
    • Christensen, L. H. (1997). Theoretical analysis of protein concentration determination using biosensor technology under conditions of partial mass transport limitation. Anal. Biochem. 249, 153-164.
    • (1997) Anal. Biochem. , vol.249 , pp. 153-164
    • Christensen, L.H.1
  • 11
    • 0027198367 scopus 로고
    • Antigen-antibody binding and masstransport by convection and diffusion to surface: A two-dimensional computer model of binding and dissociation kinetics
    • Glaser, R. W. (1993). Antigen-antibody binding and masstransport by convection and diffusion to surface: a two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213, 152-161.
    • (1993) Anal. Biochem. , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 14
    • 0023659137 scopus 로고
    • New metal chelate adsorbent's selective for proteins and peptide containing neighbouring histidine residues
    • Hochuli, E., Döbeli, H. and Schacher, A. (1987). New metal chelate adsorbent's selective for proteins and peptide containing neighbouring histidine residues. J. Chromatog. 411, 177-184.
    • (1987) J. Chromatog. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 15
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran modified gold surface for biospecific interaction analysis in surface plasmon resonance
    • Johnsson, B., Löfas, S. and Lindqvist, G. (1991). Immobilization of proteins to a carboxymethyldextran modified gold surface for biospecific interaction analysis in surface plasmon resonance. Anal. Biochem. 198, 268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfas, S.2    Lindqvist, G.3
  • 16
    • 0027517259 scopus 로고
    • Analysis of active antibody concentration. Separation of affinity and concentration parameters
    • Karlsson, R., Fagerstam, L., Nilshans, H. and Persson, B. (1993). Analysis of active antibody concentration. Separation of affinity and concentration parameters. J. Immunol. Meth. 166, 75-78.
    • (1993) J. Immunol. Meth. , vol.166 , pp. 75-78
    • Karlsson, R.1    Fagerstam, L.2    Nilshans, H.3    Persson, B.4
  • 17
    • 0010345821 scopus 로고
    • Kinetic and concentration analysis using BIA technology
    • Karlsson, R., Roos, H., Fägerstam, L. and Persson, B. (1994). Kinetic and concentration analysis using BIA technology. Methods 6, 99-110.
    • (1994) Methods , vol.6 , pp. 99-110
    • Karlsson, R.1    Roos, H.2    Fägerstam, L.3    Persson, B.4
  • 18
    • 0030583234 scopus 로고    scopus 로고
    • Determination of active single chain antibody concentrations in crude periplasmic fractions
    • Kazemier, B., de Haard, H., Boender, P., von Gemen, B. and Hoogenboom, H. R. (1996). Determination of active single chain antibody concentrations in crude periplasmic fractions. J. Immunol. Meth. 194, 201-209.
    • (1996) J. Immunol. Meth. , vol.194 , pp. 201-209
    • Kazemier, B.1    De Haard, H.2    Boender, P.3    Von Gemen, B.4    Hoogenboom, H.R.5
  • 19
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J. and Hendrickson, W. A. (1998). Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 20
    • 0028003595 scopus 로고
    • Interaction of lysozyme with synthetic anti-lysozyme D1.3 antibody fragments studied by affinity chromatography and surface plasmon resonance
    • Lasonder, E., Bloemhoff, W. and Welling, G. W. (1994). Interaction of lysozyme with synthetic anti-lysozyme D1.3 antibody fragments studied by affinity chromatography and surface plasmon resonance. J. Chromatog. A 676, 91-98.
    • (1994) J. Chromatog. A , vol.676 , pp. 91-98
    • Lasonder, E.1    Bloemhoff, W.2    Welling, G.W.3
  • 21
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons, D. S., Lieberman, S. A., Hampl, J., Boniface, J. J., Chien, Y., Berg, L. J. and Davis, M. M. (1996). A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5, 53-61.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.5    Berg, L.J.6    Davis, M.M.7
  • 22
    • 0031570325 scopus 로고    scopus 로고
    • Accurate topological comparison of two recombinant human growth hormones by optical surface resonance
    • Mani, J. C., Bras, J. M., Agut, C., Pau, B., Vita, N., Ferrara, P. and Bayol, A. (1997). Accurate topological comparison of two recombinant human growth hormones by optical surface resonance. Anal. Biochem. 248, 50-62.
    • (1997) Anal. Biochem. , vol.248 , pp. 50-62
    • Mani, J.C.1    Bras, J.M.2    Agut, C.3    Pau, B.4    Vita, N.5    Ferrara, P.6    Bayol, A.7
  • 23
    • 0021105470 scopus 로고
    • Preliminary crystallographic study of the complex between the Fab fragment of a monoclonal anti-lysozyme antibody and its antigen
    • Mariuzza, R. A., Jankovic, D. L., Boulot, G. and Amit, A. G. (1983). Preliminary crystallographic study of the complex between the Fab fragment of a monoclonal anti-lysozyme antibody and its antigen. J. Mol. Biol. 170, 1055-1058.
    • (1983) J. Mol. Biol. , vol.170 , pp. 1055-1058
    • Mariuzza, R.A.1    Jankovic, D.L.2    Boulot, G.3    Amit, A.G.4
  • 24
    • 0025325915 scopus 로고
    • A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C
    • Mateu, M. G., Martinez, M. A., Capucci, L., Andreu, D., Giralt, E., Sobrino, F., Brocchi, E. and Domingo, E. (1990). A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C. J. Gen. Virol. 71, 629-637.
    • (1990) J. Gen. Virol. , vol.71 , pp. 629-637
    • Mateu, M.G.1    Martinez, M.A.2    Capucci, L.3    Andreu, D.4    Giralt, E.5    Sobrino, F.6    Brocchi, E.7    Domingo, E.8
  • 25
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. and Pelham, H. R. (1986). An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.2
  • 27
    • 0024044173 scopus 로고
    • Genetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4
    • Peterson, A. and Seed, B. (1988). Genetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4. Cell 54, 65-72.
    • (1988) Cell , vol.54 , pp. 65-72
    • Peterson, A.1    Seed, B.2
  • 29
    • 0024339929 scopus 로고
    • Glucose as substrate in recombinant strain fermentation technology
    • Rinas, U., Kracke-Helm, H.-A. and Schugerl, K. (1989). Glucose as substrate in recombinant strain fermentation technology. Appl. Microbiol. Biotechnol. 31, 163-167.
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 163-167
    • Rinas, U.1    Kracke-Helm, H.-A.2    Schugerl, K.3
  • 31
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance by using radiolabelled proteins
    • Stenberg, E., Persson, B., Roos, H. and Urbaniczky, C. (1991). Quantitative determination of surface concentration of protein with surface plasmon resonance by using radiolabelled proteins. J. Colloid Interface Sci. 143, 513-526.
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4
  • 32
    • 0025753565 scopus 로고
    • Factors influencing inclusion body formation in the production of a fusion protein in Escherichia coli
    • Strandberg, L. and Enfors, S. O. (1991). Factors influencing inclusion body formation in the production of a fusion protein in Escherichia coli. Appl. Envir. Microbiol. 57, 1669-1674.
    • (1991) Appl. Envir. Microbiol. , vol.57 , pp. 1669-1674
    • Strandberg, L.1    Enfors, S.O.2
  • 33
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali, M., Moore, J. P., Furman, C., Charles, M., Ho, D. D., Robinson, J. and Sodroski, J. (1993). Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67, 3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 34
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trokla, A., Purtscher, M., Muster, T., Ballaun, C., Buchacher, A., Sullivan, N., Srinivasan, K., Sodroski, J., Moore, J. P. and Katinger, H. (1996). Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 70, 1100-1108.
    • (1996) J. Virol. , vol.70 , pp. 1100-1108
    • Trokla, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4    Buchacher, A.5    Sullivan, N.6    Srinivasan, K.7    Sodroski, J.8    Moore, J.P.9    Katinger, H.10
  • 35
    • 0028723878 scopus 로고
    • Use of biosensors to characterize recombinant proteins
    • Edited by Brown F. and Lubiniecki A. S., Karger, Basel
    • Van Regenmortel, M. H. V. (1994). Use of biosensors to characterize recombinant proteins. In Developments in Biological Standardization, Edited by Brown F. and Lubiniecki A. S., vol. 83, p. 143-151. Karger, Basel.
    • (1994) Developments in Biological Standardization , vol.83 , pp. 143-151
    • Van Regenmortel, M.H.V.1
  • 40
    • 0031106828 scopus 로고    scopus 로고
    • Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures
    • Zeder-Lutz, G., Zuber, E., Witz, J. and Van Regenmortel, M. H. V. (1997). Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures. Anal. Biochem. 246, 123-132.
    • (1997) Anal. Biochem. , vol.246 , pp. 123-132
    • Zeder-Lutz, G.1    Zuber, E.2    Witz, J.3    Van Regenmortel, M.H.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.