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Volumn 217, Issue 1-2, 1998, Pages 131-141

Two high-affinity monoclonal IgG2a antibodies with differing thermodynamic stability demonstrate distinct antigen-induced changes in protein A-binding affinity

Author keywords

Affinity; Differential scanning calorimetry; IgG2a antibodies; Protein A; Stability

Indexed keywords

FERRITIN; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2A; STAPHYLOCOCCUS PROTEIN A;

EID: 0032144264     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(98)00110-0     Document Type: Article
Times cited : (18)

References (34)
  • 1
    • 0022845301 scopus 로고
    • A physicochemical study of protein G, a molecule with unique immunoglobulin G-binding properties
    • Akerstrom B., Bjorck L. A physicochemical study of protein G, a molecule with unique immunoglobulin G-binding properties. J. Biol. Chem. 261:1986;10240-10247.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10240-10247
    • Akerstrom, B.1    Bjorck, L.2
  • 4
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor and Fc
    • Burmeister W.P., Huber A.H., Bjorkman P.J. Crystal structure of the complex of rat neonatal Fc receptor and Fc. Nature. 372:1994;379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 5
    • 0021857415 scopus 로고
    • Immunoglobulin functional sites
    • Burton D.R. Immunoglobulin functional sites. Mol. Immunol. 22:1985;161-206.
    • (1985) Mol. Immunol. , vol.22 , pp. 161-206
    • Burton, D.R.1
  • 6
    • 0024535597 scopus 로고
    • Dual isotope study of iodine-125 and indium-111-labeled antibody in athymic mice
    • Cartney P.L., Rogers P.E., Johnson D.K. Dual isotope study of iodine-125 and indium-111-labeled antibody in athymic mice. J. Nucl. Med. 30:1989;374-384.
    • (1989) J. Nucl. Med. , vol.30 , pp. 374-384
    • Cartney, P.L.1    Rogers, P.E.2    Johnson, D.K.3
  • 7
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 A resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 A resolution. Biochemistry. 20:1981;2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 8
    • 0017990368 scopus 로고
    • Isolation of pure IgG1, IgG2a, and IgG2b immunoglobulins from mouse serum using protein A-sepharose
    • Ey P.L., Prowse S.J., Jenkin C.R. Isolation of pure IgG1, IgG2a, and IgG2b immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry. 15:1978;429-436.
    • (1978) Immunochemistry , vol.15 , pp. 429-436
    • Ey, P.L.1    Prowse, S.J.2    Jenkin, C.R.3
  • 9
    • 0017836908 scopus 로고
    • Statistical mechanical deconvolution of thermal transitions in macromolecules: I. Theory and application to homogeneous systems
    • Freire E., Biltonen R.L. Statistical mechanical deconvolution of thermal transitions in macromolecules: I. Theory and application to homogeneous systems. Biopolymers. 17:1978;463-479.
    • (1978) Biopolymers , vol.17 , pp. 463-479
    • Freire, E.1    Biltonen, R.L.2
  • 10
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet B., Chafotte A.F., Djavadi-Ohaniance L., Goldberg M.E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Meth. 77:1985;305-319.
    • (1985) J. Immunol. Meth. , vol.77 , pp. 305-319
    • Friguet, B.1    Chafotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 11
    • 0026005140 scopus 로고
    • IgG galactosylation - Its biological significance and pathology
    • Furukawa K., Kobata A. IgG galactosylation - its biological significance and pathology. Mol. Immunol. 28:1991;1333-1342.
    • (1991) Mol. Immunol. , vol.28 , pp. 1333-1342
    • Furukawa, K.1    Kobata, A.2
  • 13
    • 0024788386 scopus 로고
    • Enhancement of the antigen-binding capacity of incomplete IgG antibodies to Brucella meltiensis through Fc region interactions with staphylococcal protein A
    • Jagannath C., Sehgal S. Enhancement of the antigen-binding capacity of incomplete IgG antibodies to Brucella meltiensis through Fc region interactions with staphylococcal protein A. J. Immunol. Meth. 124:1989;251-257.
    • (1989) J. Immunol. Meth. , vol.124 , pp. 251-257
    • Jagannath, C.1    Sehgal, S.2
  • 14
    • 0027050823 scopus 로고
    • Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast
    • Kern G., Schulke N., Schmid F.X., Jaenicke R. Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast. Prot. Sci. 1:1992;120-131.
    • (1992) Prot. Sci. , vol.1 , pp. 120-131
    • Kern, G.1    Schulke, N.2    Schmid, F.X.3    Jaenicke, R.4
  • 15
    • 0027507503 scopus 로고
    • Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae
    • Kern G., Kern D., Jaenicke R., Seckler R. Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae. Prot. Sci. 2:1993;1862-1868.
    • (1993) Prot. Sci. , vol.2 , pp. 1862-1868
    • Kern, G.1    Kern, D.2    Jaenicke, R.3    Seckler, R.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 18544403761 scopus 로고
    • Immunoaffinity methods in radiolabeling of antibodies. A critical assessment using I-125-anti-β-chorionic gonadotropin as an example
    • Li-cheng F., Andres R.Y. Immunoaffinity methods in radiolabeling of antibodies. A critical assessment using I-125-anti-β-chorionic gonadotropin as an example. J. Labeled Comp. Radiopharm. 25:1988;977-984.
    • (1988) J. Labeled Comp. Radiopharm. , vol.25 , pp. 977-984
    • Li-Cheng, F.1    Andres, R.Y.2
  • 18
    • 0021236693 scopus 로고
    • Determination of the immunoreactive fraction of radiolabeled monoclonal antibodies by linear extrapolation to binding at infinite antigen excess
    • Lindmo T., Boven E., Cuttitta F., Fedorko J., Bunn P.A. Jr. Determination of the immunoreactive fraction of radiolabeled monoclonal antibodies by linear extrapolation to binding at infinite antigen excess. J. Immunol. Meth. 72:1984;77-98.
    • (1984) J. Immunol. Meth. , vol.72 , pp. 77-98
    • Lindmo, T.1    Boven, E.2    Cuttitta, F.3    Fedorko, J.4    Bunn P.A., Jr.5
  • 19
    • 0028916303 scopus 로고
    • Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low-pH induced state
    • Martsev S.P., Kravchuk Z.I., Vlasov A.P., Lyakhnovich G.V. Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low-pH induced state. FEBS Lett. 361:1995;173-175.
    • (1995) FEBS Lett. , vol.361 , pp. 173-175
    • Martsev, S.P.1    Kravchuk, Z.I.2    Vlasov, A.P.3    Lyakhnovich, G.V.4
  • 20
    • 0028892153 scopus 로고
    • Modification of monoclonal and polyclonal IgG with palladium(II) coproporphyrin I: Stimulatory and inhibitory functional effects induced by two different methods
    • Martsev S.P., Preygerzon V.A., Mel'nikova Y.I., Kravchuk Z.I., Ponomarev G.V., Lunev V.E., Savitsky A.P. Modification of monoclonal and polyclonal IgG with palladium(II) coproporphyrin I: stimulatory and inhibitory functional effects induced by two different methods. J. Immunol. Meth. 186:1995;293-304.
    • (1995) J. Immunol. Meth. , vol.186 , pp. 293-304
    • Martsev, S.P.1    Preygerzon, V.A.2    Mel'Nikova, Y.I.3    Kravchuk, Z.I.4    Ponomarev, G.V.5    Lunev, V.E.6    Savitsky, A.P.7
  • 21
    • 0022395325 scopus 로고
    • Immunoreactivity of antimelanoma antibodies in relation to the amount of radioactive iodine substituted to the antibody molecule
    • Matzku Z., Kirchgessner H., Dipppold W.G., Bruggen J. Immunoreactivity of antimelanoma antibodies in relation to the amount of radioactive iodine substituted to the antibody molecule. Eur. J. Nucl. Med. 11:1985;260-264.
    • (1985) Eur. J. Nucl. Med. , vol.11 , pp. 260-264
    • Matzku, Z.1    Kirchgessner, H.2    Dipppold, W.G.3    Bruggen, J.4
  • 22
    • 0023147728 scopus 로고
    • A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid
    • McKiney M.M., Parkinson A. A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid. J. Immunol. Meth. 96:1987;271-275.
    • (1987) J. Immunol. Meth. , vol.96 , pp. 271-275
    • McKiney, M.M.1    Parkinson, A.2
  • 23
    • 0010299794 scopus 로고
    • Monoclonal antibodies to human spleen ferritin: II. Localization of epitopes and quantitative parameters of antigen binding
    • [Engl. Transl.]
    • Mel'nikova Y.I., Lunev V.E., Preygerzon V.A., Luneva N.M., Koshkin S.A., Rodionov M.A., Martsev S.P. Monoclonal antibodies to human spleen ferritin: II. Localization of epitopes and quantitative parameters of antigen binding. Biochemistry (Moscow). 58:1993;502-511. [Engl. Transl.].
    • (1993) Biochemistry (Moscow) , vol.58 , pp. 502-511
    • Mel'Nikova, Y.I.1    Lunev, V.E.2    Preygerzon, V.A.3    Luneva, N.M.4    Koshkin, S.A.5    Rodionov, M.A.6    Martsev, S.P.7
  • 24
    • 0019462195 scopus 로고
    • Protein A as a molecular probe for the detection of antigen induced conformational change in Fc region of rabbit antibody
    • Mota G., Moraru I., Sjoquist J., Ghetie V. Protein A as a molecular probe for the detection of antigen induced conformational change in Fc region of rabbit antibody. Mol. Immunol. 18:1981;373-378.
    • (1981) Mol. Immunol. , vol.18 , pp. 373-378
    • Mota, G.1    Moraru, I.2    Sjoquist, J.3    Ghetie, V.4
  • 25
    • 0023549782 scopus 로고
    • Human rheumatoid factors bear the internal image of the Fc binding region of staphylococcal protein A
    • Opplinger I.R., Nardella F.A., Stone G.C., Mannik M. Human rheumatoid factors bear the internal image of the Fc binding region of staphylococcal protein A. J. Exp. Med. 166:1987;702-708.
    • (1987) J. Exp. Med. , vol.166 , pp. 702-708
    • Opplinger, I.R.1    Nardella, F.A.2    Stone, G.C.3    Mannik, M.4
  • 26
    • 0017364036 scopus 로고
    • Conformational changes and complement activation induced upon antigen binding to antibodies
    • Pecht I., Ehrenburg B., Calef E., Arnon R. Conformational changes and complement activation induced upon antigen binding to antibodies. Biochem. Biophys. Res. Commun. 74:1977;1302-1310.
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 1302-1310
    • Pecht, I.1    Ehrenburg, B.2    Calef, E.3    Arnon, R.4
  • 27
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Prot. Chem. 35:1982;1-104.
    • (1982) Adv. Prot. Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 28
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov P. L, Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86:1974;665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 29
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov P.L., Potekhin S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Meth. Enzymol. 131:1986;4-51.
    • (1986) Meth. Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 31
    • 0024338370 scopus 로고
    • The Fc binding site for streptococcal protein G is the Cγ2-Cγ3 interface region of IgG and is related to the sites that bind staphylococcal protein A and human rheumatoid factors
    • Stone G.C., Sjobring U., Bjork L., Sjoquist J., Barber C.V., Nardella F.A. The Fc binding site for streptococcal protein G is the Cγ2-Cγ3 interface region of IgG and is related to the sites that bind staphylococcal protein A and human rheumatoid factors. J. Immunol. 143:1989;565-570.
    • (1989) J. Immunol. , vol.143 , pp. 565-570
    • Stone, G.C.1    Sjobring, U.2    Bjork, L.3    Sjoquist, J.4    Barber, C.V.5    Nardella, F.A.6
  • 33
    • 0025124512 scopus 로고
    • Inhibition of autoradiolysis of radiolabeled monoclonal antibodies by cryopreservation
    • Wahl R.L., Wissing J., del Rosario R., Zasadny K.R. Inhibition of autoradiolysis of radiolabeled monoclonal antibodies by cryopreservation. J. Nucl. Med. 30:1990;84-89.
    • (1990) J. Nucl. Med. , vol.30 , pp. 84-89
    • Wahl, R.L.1    Wissing, J.2    Del Rosario, R.3    Zasadny, K.R.4
  • 34
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure
    • Wright A., Tao M., Kabat E.A., Morrison A.L. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J. 10:1991;2717-2723.
    • (1991) EMBO J. , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.2    Kabat, E.A.3    Morrison, A.L.4


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