메뉴 건너뛰기




Volumn 33, Issue 13, 1996, Pages 1067-1077

Effects of secondary forces on the ligand binding properties and variable domain conformations of a monoclonal anti-fluorescyl antibody

Author keywords

D12KFl; dH2O; Distilled water; E12KFl; Monofluoresceinated polyarginine (R6 FKl R6); Monofluoresceinated polyarginine polyaspartic acid (R6 KFl D6); Monofluoresceinated polyaspartic acid (D6 KFl D6); Monofluoresceinated polyglutamic acid (E6 KFl E6); R12KFl; R6D6KFl

Indexed keywords

FLUORESCEIN; MONOCLONAL ANTIBODY; SYNTHETIC PEPTIDE;

EID: 0030237630     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(96)00066-1     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0026641493 scopus 로고
    • Quenching of fluorescein conjugated lipids by antibodies: Quantitative recognition and binding of lipid-bound haptens in biomembrane models, formation of two-dimensional protein domains and molecular dynamics simulations
    • Ahlers M., Grainger D. W., Herron J. N., Lim K., Ringsdorf H. and Salesse C. (1992) Quenching of fluorescein conjugated lipids by antibodies: quantitative recognition and binding of lipid-bound haptens in biomembrane models, formation of two-dimensional protein domains and molecular dynamics simulations. Biophys. J. 63, 823-838.
    • (1992) Biophys. J. , vol.63 , pp. 823-838
    • Ahlers, M.1    Grainger, D.W.2    Herron, J.N.3    Lim, K.4    Ringsdorf, H.5    Salesse, C.6
  • 2
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari A., Jones C. M., Henry E. R., Hofrichter J. and Eaton W. A. (1992) The role of solvent viscosity in the dynamics of protein conformational changes. Science 256, 1796-1798.
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 3
    • 0024537949 scopus 로고
    • Comparison of variable region primary structures with an anti-fluorescein idiotype family
    • Bedzyk W. D., Johnson L. S., Riordan G. S. and Voss E. W. Jr (1989) Comparison of variable region primary structures with an anti-fluorescein idiotype family. J. Biol. Chem. 264, 1565-1569.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1565-1569
    • Bedzyk, W.D.1    Johnson, L.S.2    Riordan, G.S.3    Voss E.W., Jr.4
  • 4
    • 0017595073 scopus 로고
    • Structural and dynamical aspects of membrane immunochemistry using model membranes
    • Brulet P. and McConnell H. M. (1977) Structural and dynamical aspects of membrane immunochemistry using model membranes. Biochemistry 16, 1209-1217.
    • (1977) Biochemistry , vol.16 , pp. 1209-1217
    • Brulet, P.1    McConnell, H.M.2
  • 5
    • 0025784057 scopus 로고
    • Single-chain site-specific mutations of fluorescein-amino acid contact residues in high affinity monoclonal antibody 4-4-20
    • Denzin L. K., Whitlow M. and Voss E. W. Jr (1991) Single-chain site-specific mutations of fluorescein-amino acid contact residues in high affinity monoclonal antibody 4-4-20. J. Biol. Chem. 266, 14095-14103.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14095-14103
    • Denzin, L.K.1    Whitlow, M.2    Voss E.W., Jr.3
  • 6
    • 0028237951 scopus 로고
    • Investigation of specific binding of antifluorescyl antibody and Fab to fluorescein lipids in Langmuir-Blodgett deposited films using quartz microbalance methodology
    • Ebato H., Gentry C. A., Herron J. N., Muller W., Okahata Y., Ringsdorf H. and Succi P. A. (1994) Investigation of specific binding of antifluorescyl antibody and Fab to fluorescein lipids in Langmuir-Blodgett deposited films using quartz microbalance methodology. Analyt. Chem. 66, 1683-1689.
    • (1994) Analyt. Chem. , vol.66 , pp. 1683-1689
    • Ebato, H.1    Gentry, C.A.2    Herron, J.N.3    Muller, W.4    Okahata, Y.5    Ringsdorf, H.6    Succi, P.A.7
  • 8
    • 0029647450 scopus 로고
    • Protein reaction kinetics in a room-temperature glass
    • Hagen S. J., Hofrichter J. and Eaton W. A. (1995) Protein reaction kinetics in a room-temperature glass. Science 269, 959-962.
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 9
    • 0002233983 scopus 로고
    • Equilibrium kinetic methodology for the measurement of binding properties in monoclonal and polyclonal populations of antifluorescyl-IgG antibodies
    • (Edited by Voss E. W. Jr), CRC Press, Boca Raton
    • Herron J. N. (1984) Equilibrium kinetic methodology for the measurement of binding properties in monoclonal and polyclonal populations of antifluorescyl-IgG antibodies. In Fluorescein Hapten: An Immunological Probe (Edited by Voss E. W. Jr), pp. 50-75. CRC Press, Boca Raton.
    • (1984) Fluorescein Hapten: An Immunological Probe , pp. 50-75
    • Herron, J.N.1
  • 10
    • 0024329804 scopus 로고
    • Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol
    • Herron J. N., He X-m., Mason M. L., Voss E. W. Jr and Edmundson A. B. (1989) Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol. Prot. Struct. Funct. Genet. 5, 271-280.
    • (1989) Prot. Struct. Funct. Genet. , vol.5 , pp. 271-280
    • Herron, J.N.1    He, X.-M.2    Mason, M.L.3    Voss E.W., Jr.4    Edmundson, A.B.5
  • 11
    • 0023047641 scopus 로고
    • Thermodynamic properties of ligand binding by monoclonal and anti-fluorescyl antibodies
    • Herron J. N., Kranz D. M., Jameson D. M. and Voss E. W. Jr (1986) Thermodynamic properties of ligand binding by monoclonal and anti-fluorescyl antibodies. Biochemistry 25, 4602-4609.
    • (1986) Biochemistry , vol.25 , pp. 4602-4609
    • Herron, J.N.1    Kranz, D.M.2    Jameson, D.M.3    Voss E.W., Jr.4
  • 12
    • 0028046701 scopus 로고
    • High resolution structures of the 4-4-20 Fab fluorescein complex in two solvent systems: Effects of solvent on structure and antigen-binding affinity
    • Herron J. N., Terry A. H., Johnson S., He X-m., Gudday L. W., Voss E. W. Jr and Edmundson A. B. (1994) High resolution structures of the 4-4-20 Fab fluorescein complex in two solvent systems: effects of solvent on structure and antigen-binding affinity. Biophys. J. 67, 2167-2183.
    • (1994) Biophys. J. , vol.67 , pp. 2167-2183
    • Herron, J.N.1    Terry, A.H.2    Johnson, S.3    He, X.-M.4    Gudday, L.W.5    Voss E.W., Jr.6    Edmundson, A.B.7
  • 13
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks W. P. (1981) On the attribution and additivity of binding energies. Proc. natn. Acad. Sci. U.S.A. 78, 4046-4050.
    • (1981) Proc. Natn. Acad. Sci. U.S.A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 14
    • 0026529042 scopus 로고
    • Fluorescence quenching measurements of the membrane bound lipid haptens with different length haptens
    • Kimura K., Arata Y., Yasuda T., Kinosita K. Jr and Nakanishi M. (1992) Fluorescence quenching measurements of the membrane bound lipid haptens with different length haptens. Biochim. Biophys. Acta 1104, 9-14.
    • (1992) Biochim. Biophys. Acta , vol.1104 , pp. 9-14
    • Kimura, K.1    Arata, Y.2    Yasuda, T.3    Kinosita K., Jr.4    Nakanishi, M.5
  • 15
    • 0000755325 scopus 로고
    • Partial elucidation of an anti-hapten repertoire in Balb/c mice: Comparative characterization of several monoclonal anti-fluorescyl antibodies
    • Kranz D. M. and Voss E. W. Jr (1981) Partial elucidation of an anti-hapten repertoire in Balb/c mice: comparative characterization of several monoclonal anti-fluorescyl antibodies. J. Biol. Chem. 257, 6987-6995.
    • (1981) J. Biol. Chem. , vol.257 , pp. 6987-6995
    • Kranz, D.M.1    Voss E.W., Jr.2
  • 16
    • 0027410832 scopus 로고
    • The basics of binding: Mechanisms of antigen recognition and mimicry by antibodies
    • Mariuzza R. A. and Poljak R. J. (1993) The basics of binding: mechanisms of antigen recognition and mimicry by antibodies. Curr. Opin. Immun. 5, 50-55.
    • (1993) Curr. Opin. Immun. , vol.5 , pp. 50-55
    • Mariuzza, R.A.1    Poljak, R.J.2
  • 17
    • 0029557832 scopus 로고
    • Effects of secondary forces on the primary antibody-ligand interaction
    • Mummert M. E. and Voss E. W. Jr (1995) Effects of secondary forces on the primary antibody-ligand interaction. Molec. Immun. 32, 1225-1233.
    • (1995) Molec. Immun. , vol.32 , pp. 1225-1233
    • Mummert, M.E.1    Voss E.W., Jr.2
  • 18
    • 0024605425 scopus 로고
    • Immunochemistry at interfaces
    • Nygren H. and Stenberg M. (1989) Immunochemistry at interfaces. Immunology 66, 321-327.
    • (1989) Immunology , vol.66 , pp. 321-327
    • Nygren, H.1    Stenberg, M.2
  • 19
    • 0027366723 scopus 로고
    • Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens
    • Ong G. L. and Mattes M. J. (1993) Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens. Molec. Immun. 30, 1455-1462.
    • (1993) Molec. Immun. , vol.30 , pp. 1455-1462
    • Ong, G.L.1    Mattes, M.J.2
  • 20
    • 0028935073 scopus 로고
    • Hydrophobic, hydrophilic and other interactions in epitope-paratope binding
    • Oss C. J. van (1995) Hydrophobic, hydrophilic and other interactions in epitope-paratope binding. Molec. Immun. 32, 199-211.
    • (1995) Molec. Immun. , vol.32 , pp. 199-211
    • Van Oss, C.J.1
  • 21
    • 0002605865 scopus 로고
    • Nature and thermodynamics of antigen-antibody interactions
    • Edited by Atassi M. Z., Oss C. J. van and Absolom D. R., Marcel Dekker, New York
    • Oss C. J. van, Absolom D. R. (1984) Nature and thermodynamics of antigen-antibody interactions. In Molecular Immunology (Edited by Atassi M. Z., Oss C. J. van and Absolom D. R., pp. 337-360. Marcel Dekker, New York.
    • (1984) Molecular Immunology , pp. 337-360
    • Van Oss, C.J.1    Absolom, D.R.2
  • 22
    • 0022454895 scopus 로고
    • Nature of the antigen-antibody interaction - Primary and secondary bonds: Optional conditions for association and dissociation
    • Oss C. J. van, Good R. J. and Chaudhury M. K. (1986) Nature of the antigen-antibody interaction - primary and secondary bonds: optional conditions for association and dissociation. J. Chromatog. 376, 111-119.
    • (1986) J. Chromatog. , vol.376 , pp. 111-119
    • Van Oss, C.J.1    Good, R.J.2    Chaudhury, M.K.3
  • 23
    • 0003354439 scopus 로고
    • Antigen-antibody reactions
    • (Edited by Van Regenmortel M. H. V.), CRC Press, Boca Raton
    • Oss C. J. van (1992) Antigen-antibody reactions. In Structure of Antigens (Edited by Van Regenmortel M. H. V.), Vol. 1, pp. 179-208. CRC Press, Boca Raton.
    • (1992) Structure of Antigens , Issue.1 , pp. 179-208
    • Van Oss, C.J.1
  • 24
    • 0002897028 scopus 로고
    • Nature of specific ligand-receptor bonds, in particular the antigen-antibody bond
    • (Edited by Oss C. J. van and Van Regenmortel M. H. V.), Marcel Dekker, New York
    • Oss C. J. van (1994) Nature of specific ligand-receptor bonds, in particular the antigen-antibody bond. In Immunochemistry (Edited by Oss C. J. van and Van Regenmortel M. H. V.), pp. 581-613. Marcel Dekker, New York.
    • (1994) Immunochemistry , pp. 581-613
    • Van Oss, C.J.1
  • 25
    • 0021754445 scopus 로고
    • Interaction of antibodies with liposomes bearing fluorescent haptens
    • Petrossian A. and Owicki J. C. (1984) Interaction of antibodies with liposomes bearing fluorescent haptens. Biochim. Biophys. Acta 776, 217-227.
    • (1984) Biochim. Biophys. Acta , vol.776 , pp. 217-227
    • Petrossian, A.1    Owicki, J.C.2
  • 26
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distribution and packing density
    • Richards F. M. (1974) The interpretation of protein structures: total volume, group volume distribution and packing density. J. Molec. Biol. 82, 1-14.
    • (1974) J. Molec. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 27
    • 0015896846 scopus 로고
    • Effect of immunoglobulin class and affinity on the initiation of complement-dependent damage to liposomal model membranes sensitized with dinitrophenylated phospholipids
    • Six H. R., Uemura K-i. and Kinsky S. C. (1973) Effect of immunoglobulin class and affinity on the initiation of complement-dependent damage to liposomal model membranes sensitized with dinitrophenylated phospholipids. Biochemistry 12, 4003-4011.
    • (1973) Biochemistry , vol.12 , pp. 4003-4011
    • Six, H.R.1    Uemura, K.-I.2    Kinsky, S.C.3
  • 28
    • 0026030432 scopus 로고
    • Fluorescence measurements of the immune complexes of Mab 4-4-20 with isomeric haptens
    • Swindlehurst C. A. and Voss E. W. Jr (1991) Fluorescence measurements of the immune complexes of Mab 4-4-20 with isomeric haptens. Biophys. J. 59, 619-628.
    • (1991) Biophys. J. , vol.59 , pp. 619-628
    • Swindlehurst, C.A.1    Voss E.W., Jr.2
  • 29
    • 0027860511 scopus 로고
    • Elucidation of anti-ssDNA autoantibody BV04-01 binding interactions with homooligonucleotides
    • Tetin S. Y., Rumbley C. A., Hazlett T. L. and Voss E. W. Jr (1993) Elucidation of anti-ssDNA autoantibody BV04-01 binding interactions with homooligonucleotides. Biochemistry 22, 9011-9017.
    • (1993) Biochemistry , vol.22 , pp. 9011-9017
    • Tetin, S.Y.1    Rumbley, C.A.2    Hazlett, T.L.3    Voss E.W., Jr.4
  • 30
    • 0001809560 scopus 로고
    • Immunological properties of fluorescein
    • (Edited by Voss E. W. Jr), CRC Press, Boca Raton
    • Voss E. W. Jr (1984) Immunological properties of fluorescein. In Fluorescein Hapten: An Immunological Probe (Edited by Voss E. W. Jr), pp. 3-13. CRC Press, Boca Raton.
    • (1984) Fluorescein Hapten: An Immunological Probe , pp. 3-13
    • Voss E.W., Jr.1
  • 31
    • 0029961080 scopus 로고    scopus 로고
    • Perturbation of antibody bound bifluorescent-ligand probe by polyclonal anti-metatype antibodies interacting with epitopes proximal to the liganded antibody active site
    • Voss E. W. Jr (1996) Perturbation of antibody bound bifluorescent-ligand probe by polyclonal anti-metatype antibodies interacting with epitopes proximal to the liganded antibody active site. Molec. Immun. 33, 79-88.
    • (1996) Molec. Immun. , vol.33 , pp. 79-88
    • Voss E.W., Jr.1
  • 32
    • 0024330380 scopus 로고
    • Inter-relationship between immunoglobulin idiotype and metatype
    • Voss E. W. Jr, Dombrink-Kurtzman M. A. and Ballard D. W. (1989) Inter-relationship between immunoglobulin idiotype and metatype. Molec. Immun. 26, 971-977.
    • (1989) Molec. Immun. , vol.26 , pp. 971-977
    • Voss E.W., Jr.1    Dombrink-Kurtzman, M.A.2    Ballard, D.W.3
  • 33
    • 0023921616 scopus 로고
    • Functional and structural implication of variable region immunoglobulin dynamic states
    • Voss E. W. Jr, Dombrink-Kurtzman M. A. and Miklasz S. D. (1988) Functional and structural implication of variable region immunoglobulin dynamic states. Immunol. Invest. 17, 25-39.
    • (1988) Immunol. Invest. , vol.17 , pp. 25-39
    • Voss E.W., Jr.1    Dombrink-Kurtzman, M.A.2    Miklasz, S.D.3
  • 34
    • 0026551753 scopus 로고
    • Importance of dynamic properties of idiotopes in interactions with anti-Id antibodies
    • Voss E. W. Jr, Weidner K. M. and Denzin L. K. (1992) Importance of dynamic properties of idiotopes in interactions with anti-Id antibodies. Immunol. Invest. 21, 71-83
    • (1992) Immunol. Invest. , vol.21 , pp. 71-83
    • Voss E.W., Jr.1    Weidner, K.M.2    Denzin, L.K.3
  • 35
    • 0017734494 scopus 로고
    • Mechanism of quenching of fluorescein by anti-fluorescein IgG antibodies
    • Watt R. M. and Voss E. W. Jr (1977) Mechanism of quenching of fluorescein by anti-fluorescein IgG antibodies. Immunochemistry 14, 533-541.
    • (1977) Immunochemistry , vol.14 , pp. 533-541
    • Watt, R.M.1    Voss E.W., Jr.2
  • 36
    • 0001908658 scopus 로고
    • Affinity labeling of antifluorescyl antibodies
    • (Edited by Voss E. W. Jr), CRC Press, Boca Raton
    • Watt R. M. and Voss E. W. Jr (1984) Affinity labeling of antifluorescyl antibodies. In Fluorescein Hapten: An Immunological Probe (Edited by Voss E. W. Jr), pp. 177-181. CRC Press, Boca Raton.
    • (1984) Fluorescein Hapten: An Immunological Probe , pp. 177-181
    • Watt, R.M.1    Voss E.W., Jr.2
  • 37
    • 0027486858 scopus 로고
    • Elicitation of distinct populations of monoclonal antibodies specific for the variable domains of monoclonal anti-fluorescein antibody 4-4-20
    • Weidner K. M., Denzin L. K., Kim M. L., Mallender W. D., Miklasz S. D. and Voss E. W. Jr (1993) Elicitation of distinct populations of monoclonal antibodies specific for the variable domains of monoclonal anti-fluorescein antibody 4-4-20. Molec. Immun. 30, 1003-1011.
    • (1993) Molec. Immun. , vol.30 , pp. 1003-1011
    • Weidner, K.M.1    Denzin, L.K.2    Kim, M.L.3    Mallender, W.D.4    Miklasz, S.D.5    Voss E.W., Jr.6
  • 38
    • 0025734126 scopus 로고
    • Immunological characterization of xenogenic anti-metatype antibodies
    • Weidner K. M. and Voss E. W. Jr (1991) Immunological characterization of xenogenic anti-metatype antibodies. J. Biol. Chem. 266, 2513-2519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2513-2519
    • Weidner, K.M.1    Voss E.W., Jr.2
  • 39
    • 0026547939 scopus 로고
    • Characterization of interactions involving anti-metatype antibodies and immune complexes
    • Weidner K. M. and Voss E. W. Jr (1992) Characterization of interactions involving anti-metatype antibodies and immune complexes. Molec. Immun. 29, 303-312.
    • (1992) Molec. Immun. , vol.29 , pp. 303-312
    • Weidner, K.M.1    Voss E.W., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.