Thermodynamics of hCG-monoclonal antibody interaction: An analysis of real time kinetics data obtained using radiolabeled hCG probe

Biochimica et Biophysica Acta - General Subjects

Volumn 1572, Issue 1, 2002, Pages 31-36

  Ashish, Banerjee ^a   Tamil Selvi, P ^a   Murthy, Gundlupet Satyanarayana ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Antigen antibody; Human chorionic gonadotropin; Real time kinetics; Thermodynamics

Indexed keywords

CHORIONIC GONADOTROPIN; IODINE 125; MONOCLONAL ANTIBODY;

ANTIGEN BINDING; ARTICLE; CALCULATION; DATA ANALYSIS; DISSOCIATION; ENERGY TRANSFER; ENTHALPY; ENTROPY; EQUILIBRIUM CONSTANT; HYDROPHOBICITY; ISOTOPE LABELING; MATHEMATICAL ANALYSIS; MOLECULAR PROBE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; TEMPERATURE; THERMODYNAMICS;

ANTIBODIES, MONOCLONAL; ANTIGEN-ANTIBODY REACTIONS; CHORIONIC GONADOTROPIN; IODINE RADIOISOTOPES; KINETICS; TEMPERATURE; THERMODYNAMICS;

EID: 0037104625     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00274-X     Document Type: Article

References (27)

1. Venkatesh N., Im S.H., Balass M., Fuchs S., Katchalski-Katzir E. Prevention of passively transferred experimental autoimmune myasthenia gravis by a phage library-derived cyclic peptide. Proc. Natl. Acad. Sci. U. S. A. 97:2000;761-766.
2. Kam-Morgan L.N.W., Smith-Gill S.J.S., Taylor M.G., Zhang L., Wilson A.C., Kirsch J.F. High resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site directed mutagenesis. Proc. Natl. Acad. Sci. U. S. A. 90:1993;3958-3962.
3. Nandi A., Suguna K., Surolia A., Visweswariah S.S. Topological mimicry and epitope duplication in the guanylyl cyclase C receptor. Protein Sci. 10:1998;2175-2183.
4. Venkatesh N., Krishnaswami S., Meuris S., Murthy G.S. Epitope analysis and molecular modeling reveal the topography of the C-terminal peptide of the β subunit of human chorionic gonadotropin. Eur. J. Biochem. 265:1999;1061-1066.
5. Padlan E.A., Silverton E.W., Sheriff S., Cohen G.H., Smith-Gill S.J., Davies D.R. Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-Lysozyme complex. Proc. Natl. Acad. Sci. U. S. A. 86:1989;5938-5942.
6. Colman P.M., Tulip W.R., Varghese J.N., Tulloch P.A., Baker A.T., Laver W.G., Air G.M., Webster R.G. Three-dimensional structure of influenza virus neuraminidase-antibody complexes. Philos. Trans. R. Soc. Lond., B. 323:1989;511-518.
7. Novotny J. Protein antigenicity: a thermodynamic approach. Mol. Immunol. 28:1991;201-207.
8. Schillbach J.F., Near R.I., Bruccoleri R.E., Haber E., Jeffrey P.D., Novotny J., Sheriff S., Margolies M.N. Modulation of antibody affinity by a non-contact residue. Protein Sci. 2:1993;206-214.
9. Chothia C., Lesk A.M., Levitt M., Amit A.G., Mariuzza R.A., Phillips S.E., Poljak R.J. The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure. Science. 233:1986;755-758.
10. Varadarajan R., Connelly P.R., Sturtevant J.M., Richards F.M. Heat capacity changes for protein-peptide interactions in the ribonuclease S system. Biochemistry. 31:1992;1421-1426.
11. Sturtevant J.M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. U. S. A. 74:1977;2236-2240.
12. Faiman G.A., Horovitz A. Thermodynamic analysis of the interaction between the 0.5β Fv fragment and the RP135 peptide antigen derived from the V3 loop of HIV-1 gp-120. J. Biol. Chem. 272:1997;331407-331411.
13. Wiseman T., Williston S., Brandts J.F., Lin L. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
14. Swaminathan C.P., Nandi A., Visweswariah S.S., Surolia A. Thermodynamic analysis reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor. J. Biol. Chem. 274:1999;31272-31278.
15. Torigoe H., Nakayama T., Imazato M., Shimada I., Arata Y., Sarai A. The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. J. Biol. Chem. 270:1995;22218-22222.
16. Murthy G.S. Determination of kinetic parameters and thermodynamic constant of antigen-antibody reaction by solid phase binding method. Curr. Sci. (India). 73:1997;1097-1103.
17. Murthy G.S. Realtime kinetic analysis of antigen-antibody interaction using solid phase binding: transformation of hCG-monoclonal antibody complex. Curr. Sci. (India). 71(12):1996;981-988.
18. Banerjee A., Srilatha N.S., Murthy G.S. Real-time kinetic analysis of hCG-monoclonal antibody interaction using radiolabeled hCG probe: presence of two forms of Ag-MAb complex as revealed by solid phase dissociation studies. Biochim. Biophys. Acta. 1569:2002;21-30.
19. Murthy G.S., Moudgal N.R. Use of epoxy sepharose for protein immobilisation. J. Biosci. (India). 10(3):1986;351-358.
20. Fraker P.J., Speck J.C. Protein and cell membrane iodination with sparingly soluble chloramide 1,3,4,6-tetra chloro-3, 6-diphenyl glycouril. Biochem. Biophys. Res. Commun. 80:1978;849-857.
21. Srilatha N.S., Murthy G.S. Study of dissociation of human chorionic gonadotropin monoclonal antibody complexes using nitrocellulose as an insoluble support. Curr. Sci. (India). 78(12):2000;1548-1552.
22. Raman C.S., Allen M.J., Nall B.T. Enthalpy of antibody-cytochrome c binding. Biochemistry. 34:1995;5831-5838.
23. Gomez J., Freire E. Thermodynamic mapping of the inhibitor site of the aspartic protease Endothiapepsin. J. Mol. Biol. 252:1995;337-350.
24. Baker B.M., Murphy K.P. Dissecting the energetics of a protein-protein interaction: the binding of Ovomucoid third domain to Elastase. J. Mol. Biol. 268:1997;557-569.
25. Spolar R.S., Record M.T. Jr. Coupling of local folding to site specific binding of proteins to DNA. Science. 263:1994;777-784.
26. Venkatesh N., Murthy G.S. Immunochemical approach to the mapping of an assembled epitope of human chorionic gonadotropin: proximity of CTP-α to the receptor binding region of the β-subunit. J. Immunol. Methods. 202:1997;173-182.
27. Venkatesh N., Murthy G.S. Stability of assembled epitopes on human chorionic gonadotropin to covalent modification: analysis using monoclonal antibody probes. Int. J. Biochem. Mol. Biol. 42(4):1997;853-863.