Determination of kinetic parameters and thermodynamic constant of antigen-antibody reaction by solid phase binding method

Study of the dissociation of [I-125]hCG from immobilized MAb-[I-125]hCG complex was carried out. The dissociation data fitted into a two-step reaction mechanism of the interaction. Kinetic parameters obtained were consistent, and were used to obtain the thermodynamic constants of the interaction. The first step (epitope recognition reaction) was shown to be a high-affinity intermolecular binding reaction involving epitope-paratope interaction, while the transformation reaction (second step) is an intramolecular rearrangement of the [I-125]hCG-MAb complex formed in the first step. The method described has the potential to be automated