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https://doi.org/10.37358/Rev.Chim.1949

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Revista de Chimie (Rev. Chim.), Year 2007, Volume 58, Issue 3,





Evaluation of Kinetic and Thermodynamic Parameters for
Antigen-Antibody Interactions by ELISA Technique

Abstract:

One evaluated by immunoenzymatic technique (ELISA) the thermodynamic parameters, affinity constant and site numbers of the following antigen - antibody systems: IBR, NDV and EDS viruses - specific sera to these antigens. The IBR systems showed two types of binding: uni and bivalent ones. The affinity is much stronger for the univalent complex in comparison to the bivalent one. For the same antigen, high positive serum has higher affinity constant than the weak positive serum. We also evaluated the kinetic parameters - rate constants - of these processes by the same ELISA technique. The antibodies from the high positive serum interact faster with the IBR antigen in comparison with those from weak positive serum. The other two systems we studied presented the same behaviour. Keywords: antigen, antibody, affinity constant, rate constant, ELISA


Issue: 2007, Volume 58, Issue 3
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