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Kinetics of Antibody-Hapten Interactions

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Chemical Relaxation in Molecular Biology

Part of the book series: Molecular Biology Biochemistry and Biophysics ((MOLECULAR,volume 24))

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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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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  • DOI: https://doi.org/10.1007/978-3-642-81117-3_9

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