Abstract
The BIACORE system, differential titration calorimetry (DTC) and a stoppedflow instrument have been used for measurement of physico-chemical constants associated with antigen-antibody interactions. After mutations were systematically introduced into the complementarity-determining regions (CDRs) of antibody that correspond to its antigen-binding site, the effects of mutations on its antigen-binding activity were physico-chemically analyzed. Since antigen-antibody interactions are reversible as shown by the following equation,
they must obey the rules of thermodynamics as well as the rules of kinetics. The following three equations show the relationships between rate constants (association rate constant k a, dissociation rate constant k d) and an equilibrium constant (affinity constant K A) as well as the relationships among thermodynamic parameters (∆G, ∆H, ∆S).
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Kurosawa, Y., Shimada, I., Williams, C., Shimada, I., Arisaka, F. (2000). Combinations with Other Methods. In: Nagata, K., Handa, H. (eds) Real-Time Analysis of Biomolecular Interactions. Springer, Tokyo. https://doi.org/10.1007/978-4-431-66970-8_20
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DOI: https://doi.org/10.1007/978-4-431-66970-8_20
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