Abstract
The immune system, which is the major defence complex present in vertebrates against foreign cells and pathogens, is comprised of lymphocytes and their products, the antibodies. The latter carry out the function of recognition of antigenic determinants and the resultant triggering of a wide range of biological responses. Antibodies are all immunoglobulins - a group of multichain proteins whose similar gross structure may be expressed as (HL)2n where H and L are the heavy and light polypeptide chains, respectively, linked together by noncovalent and disulfide bonds. For the IgG class n = 1 and,for the IgM class n = 5. The light chains are 22,500 daltons whereas the heavy chainsary according to class between 53,000 for the IgG to 75,000 daltons for IgE (EDELMAN and GALL, 1969). A typical property of antibodies, even from one individual animal and having the same specificity, is the pronounced heterogeneity found in their primary structure. This heterogeneity is confined, however, to the first 110 N-terminal residues of the two chains (variable region) and expresses the diversity of the antigen combining site. Certain stretches in the variable region were found to exhibit higher variability, and these hypervariable residues were proposed to form the main contact areas of the binding site (RABAT and WU, 1971). X-ray crystallography has verified this hypothesis (DAVIES et al., 1976; POLJAK, 1975).
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References
ALBERTY, R.A., HAMMES, G.G.: Application of the theory of diffusion-controlled reactions to enzyme kinetics. J. Phys. Chem. 62, 154–159 (1958)
BARISAS, B.G., SINGER, S.J., STURTEVANT, J.M.: Thermodynamics of the binding of 2,4 dinitrophenyl and 2,4,6-trinitrophenyl haptens to the homologous and heterologous rabbit antibodies. Biochemistry 11, 2741–2744 (1972)
BARISAS, B.G., SINGER, S.J., STURTEVANT, J.M.: Kinetic evidence for a conformational change by an anti-hapten antibody upon binding multivalent hapten. Abstr. 9th Intern. Corigr. Biochemistry, Stockholm, 312 (1973)
BARISAS, B.G., SINGER, S.J., STURTEVANT, J.M.: Kinetics of binding of 2,4 dinitrophenyl and 2,4,6-trinitrophenyl haptens to homologous and heterologous rabbit antibodies. Immunochemistry 12, 411–421 (1975)
BERSON, S.A., YALOW, R.S.: Quantitative aspects of the reaction between insulin and insulin-binding antibody. J. Clin. Invest. 38, 1996–2016 (1959)
BLATT, Y., KARUSH, F., PECHT, I.: unpublished (1976)
CASTELLAN, G.W.: Calculation of the spectrum of chemical relaxation times for a general reaction mechanism. Berich. Bunsenges. 67, 898–908 (1963)
DANDLIKER, W.B., LEVISON, S.A.: Investigation of antigen-antibody kinetics. Immunochemistry 5, 171–183 (1968)
DAVIES, D.R., PADLAN, E.A., SEGAL, D.M.: Immunoglobulin structures at high resolution. Contemp. Topics Mol. Immunol. 4, 12 7–155 (1975)
DAY, L.A., STURTEVANT, J.M., SINGER, S.J.: The kinetics of the reactions between antibodies to the 2,4 dinitrophenyl group and specific haptens. Ann. N.Y. Acad. Sci. 103, 611–625 (1963)
EDELMAN, G.M., GALL, W.E.: The antibody problem. Ann. Rev. Biochem. 18, 415–466 (1969)
EIGEN, M.: Diffusion control in biochemical reactions. In: Quantum statistical mechanics in the nature sciences. MINTZ, S.L., WIEDERMAYER, S.M. (eds.). New York: Plenum Press 1974, p.37–61
EIGEN, M., DE MAEYER, L.: Theoretical basis of relaxation spectrometry. In: Techniques of Chemistry. WEISSBERGER, A., HAMMES, G.G. (eds.); Vol. VI, Part 2, p. 63–146. New York: Wiley 1973
EISEN, H.N., SIMMS, E.S., POTTER, M.: Mouse myeloma proteins with anti-hapten antibody activity: The protein produced by plasma cell tumor MOPC 315. Biochemistry 7, 4126–4134 (1968)
FROESE, A.: Kinetic and equilibrium studies on 2,4 dinitrophenyl hapten-antibody systems. Immunochemistry 5, 253–264 (1968)
FROESE, A., SEHON, A.H.: Kinetic and equilibrium studies of the reaction between anti-p-nitrophenyl antibodies and a homologous hapten. Immunochemistry 2, 135–143 (1965)
FROESE, A., SEHON, A.H.: Kinetics of antibody-hapten reactions. Contemp. Topics Mol. Immunol. 4, 23–54 (1975)
FROESE, A., SEHON, A.H., EIGEN, M.: Kinetic studies on proteindye and antibody hapten interactions with the temperature-jump method. Can. J. Chem. 40, 1786–1797 (1962)
GLASSTONE, S.: Textbook of Physical Chemistry. Princeton: Van Nostrand 1946
GÖTZE, O., MÜLLER EBERHARD, J.: The C3-activator system: an alternate pathway to complement activation. J. Exp. Med. 134, 90S-108S (1971)
HAMMES, G.G., SCHIMMEL, P.R.: Rapid reactions and transient states. In: The Enzymes. BOYER, P.D. (ed.); Vol. II, 3rd ed., pp. 112. New York: Academic Press 1970
HARISDANGKUL, V., RABAT, E.A.: Interaction of 1-(m-nitrophenyl) flavazoles of isomaltose oligosaccharides with purified antidextran. J. Immunol. 108, 1232–1243 (1972)
HARTMANN, U., PECHT, I.: unpublished data
HASELKORN, D.: Ph.D Thesis Feinberg Graduate School, The Weizmann Inst. Sci., Rehovot, Israel (1975)
HASELKORN, D., FRIEDMAN, S., GIVOL, D., PECHT, I.: Kinetic mapping of the antibody combining site by chemical relaxation spectrometry. Biochemistry 13, 2210–2222 (1974)
HAUSTEIN, D.: Dissertation, Univ. Freiburg, W. Germany (1971)
HSIA, J.C., RUSSEL LITTLE, J.: Structural properties of the ligand binding sites of murine myeloma proteins. FEBS Lett. 31, 80–84 (1973)
HUBER, R., DEISENHOFER, J., COLMAN, P., MATSUSHIMA, M., PALM, W.: X-ray diffraction analysis of immunoglobulin structure. 27th Mosbach Coll. Berlin-Heidelberg-New York: Springer 1976
INBAR, D., HOCHMAN, J., GIVOL, D.: Localization of antibody combining sites within the variable portions of heavy and light chains. Proc. Nat. Acad. Sci. (Wash.) 69, 2659–2664 (1972)
JAFFE, B.M., SIMMS, E.S., EISEN, H.N.: Specificity and structure of the myeloma protein produced by mouse plasmacytoma MOPC 460. Biochemistry 10, 1693–1699 (1971)
JENCKS, W.P.: Binding Energy, Specificity, and Enzymic Catalysis: The circe effect. Advan. Enzymol. 43, 219–410 (1975)
JOHNSTON, M.F.M., BARISAS, B.G., STURTEVANT, J.M.: Thermodynamics of hapten binding to MOPC 315 and MOPC 460 mouse myeloma proteins. Biochemistry 34, 390–396 (1974)
JOVIN, T.: Fluorimetric kinetic techniques: Chemical relaxation and stopped-flow. In: Biochemical Fluorescence/Concepts. CHEN, R.F., EDELHOCH, H.: (eds.); Vol. I, pp. 305–374. New York: Dekker 1975
RABAT, E.A.: The nature of the antigenic determinant. J. Immunol. 97, 1–11 (1966)
RABAT, E.A., WU, T.T.: Attempts to locate complementarity determining residues in the variable positions of light and heavy chains. Ann. N.Y. Acad. Sci. 190, 382–390 (1971)
KARUSH, F.: The affinity of antibody: Range, variability and the role of multivalence. In: Comprehensive Immunology (in press, 1976).
KAUZMANN, W.: Some factors in the interpretation of protein de- naturation. Advan. Protein Chem. 14, 1–13 (1959)
KELLY, K.A., SEHON, A.H., FROESE, A.: Kinetic studies on antibodyhapten reactions. Immunochemistry 8, 613–625 (1971)
LANCET, D., KABAT, E.A., PECHT, I.: unpublished data.
LANCET, D., PECHT, I.: Kinetic evidence for hapten induced conformational transition in immunoglobulin MOPC 460. Proc. Nat. Acad. Sci. (Wash.) 73, 3548–3553 (1976)
LEE, F.H., FROESE, A.: Kinetics of the reaction between DNP Insulin and homologous antibody. Immunol. Comm. 2, 565–571 (1973)
LEVISON, S.A., HICKS, A.N., PORTMANN, A.J., DANDLIKER, W.B.: Fluorescence polarization and intensity kinetic studies of anti-fluorescein antibody obtained at different stages of immune response. Biochemistry 14, 3778–3786 (1975)
LEVISON, S.A., JANCSI, A.N., DANDLIKER, W.B.: Temperature effects on the kinetics of the primary antigen-antibody combination. Biochem. Biophys. Res. Comm.,33, 942–948 (1968)
LONGSWORTH, L.E.: Temperature dependence of diffusion in aqueous solutions. J. Phys. Chem. 58, 770–773 (1954)
METZGER, H.: Effect of antigen binding on the properties of antibody. Advan. Immunol. 18, 167–207 (1974)
MONOD, J., WYMAN, J., CHANGEUX, J.P.: On the nature of allosteric transitions: A plaüsible model. J. Mol. Biol. 12, 88–118 (1965)
NOBLE, R.W., REICHLIN, M., GIBSON, Q.H.: The reactions of antibodies with hemoprotein antigens. J. Biol. Chem. 244, 2403–2411 (1969)
NOBLE, R.W., REICHLIN, M., SCHREIBER, R.D.: Studies on antibodies directed towards antigenic sites on globular proteins. Biochemistry 11, 3326–3332 (1972)
NORTH, A.M.: The Collision Theory of Chemical Reactions in Liquids. New York: Methuen 1964
PADLAN, E.A., DAVIS, D.R., PECHT, I., GIVOL, D., WRIGHT, C.E.: Model building studies of antigen binding sites: The hapten binding site of MOPC-315. Cold Spring Harbor Symp. Quant. Biol. Vol. XLI (1977)
PECHT, I.: Antibody combining sites as a model for molecular recognition. In: Protein-Ligand Interactions. SUND, H., BLAUER, G. (eds.); pp. 356–371. Berlin: de Gruyter 1975
PECHT, I., GIVOL, D., SELA, M.: Dynamics of antiboy-hapten interaction. Studies on a myeloma protein with anti DNP specificity. J. Mol. Biol. 68, 241–247 (1972)
PECHT, I., HASELKORN, D., FRIEDMAN, S.: Kinetic mapping of antibody binding sites by chemical relaxation spectrometry. FEBS Lett. 24, 331–334 (1972)
POLJAK, R.: X-ray diffraction studies of immunoglobulins. Advan. Immunol. 21, 1–33 (1975)
ROSENSTEIN, W.R., MUSSON, R.A., ARMSTRONG, M.Y.K., KÖNIGSBERG, W.A., RICHARDS, F.F.: Contact regions for DNP and menadione haptens in an immunoglobulin binding more than one antigen. Proc. Nat. Acad. Sci. (Wash.) 69, 877–881 (1972)
SACHS, D.H., SCHECHTER, A.N., EASTLAKE, A., ANFINSEN, C.B.: In- activation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic site. Biochemistry 1, 4268–4273 (1972)
SCHLESSINGER, J., STEINBERG, I.Z., GIVOL, D., HOCHMAN, J., PECHT, I.: Antigen-induced conformational changes in antibodies and their Fab fragments studied by circular polarization of fluo-rescence. Proc. Nat. Acad. Sci. (Wash.) 72, 2775–2779 (1975)
SMITH, T.W., SKUBITZ, K.M.: Kinetics of interactions between antibodies and haptens. Biochemistry 14, 1496–1502 (1975)
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Pecht, I., Lancet, D. (1977). Kinetics of Antibody-Hapten Interactions. In: Pecht, I., Rigler, R. (eds) Chemical Relaxation in Molecular Biology. Molecular Biology Biochemistry and Biophysics, vol 24. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81117-3_9
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