AI Article Synopsis
- The Langmuir equation was used to optimize ELISA data, linking the maximum response to full antigen binding and the half-maximum response to the dissociation constant, reflecting antibody affinity.
- The algorithm effectively analyzed antibody-antigen systems, showing good correlation between experimental data and theoretical predictions, with valid affinity constants.
- It also investigated IgG, IgM, and IgA antibodies binding to a polysaccharide antigen during vaccine testing, uncovering two main epitopes and their antibody formation dynamics.
Article Abstract
The use of the Langmuir equation for processing ELISA data (the sandwich variant) helped to ascribe a physical sense to the parameters of the optimization of the antigen-antibody titration curve: the maximum response that characterizes complete binding corresponds to the saturation of all epitopes of the antigen, and the concentration at which half of the maximum response is attained corresponds to the dissociation constant of the immune complex, i.e., to the average affinity of the antibodies. The algorithm was tested for systems in which antibodies against IgE and IgD were sorbed on a support, and the antigen bound was determined by the antibodies conjugated with peroxidase. A good fit of the experimental and theoretical curves and reasonable values for the affinity constants were found. In another system, the binding of specific IgG, IgM, and IgA antibodies with the polysaccharide from Neisseria meningitidis serotype A was studied during vaccine testing. The structural simplicity of the antigen molecule made it possible to suggest the presence of two main epitopes and to reveal the dynamics of formation of the antibodies to them.
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