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[Interaction between immobilized antibodies and the antigen-enzyme complex].

B B Dzantiev, E M Gavrilova, A M Egorov

    Biokhimiia (Moscow, Russia)
    |February 1, 1979
    PubMed
    Summary

    Immobilized antibodies reversibly bind to human immunoglobulin G (IgG)-peroxidase complexes, mimicking solution-based reactions. Binding efficiency is high, with constants around 4.2 x 10^8 M-1, regardless of immobilization method.

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    Area of Science:

    • Biochemistry
    • Immunology
    • Bioconjugation

    Context:

    • Antibody immobilization is crucial for immunoassays and biosensors.
    • Understanding the binding kinetics of antibody-antigen interactions is essential for optimizing assay performance.
    • Immunoenzyme complexes, like IgG-peroxidase, are widely used in diagnostic applications.

    Purpose:

    • To investigate the interaction between immobilized antibodies and an immunoenzyme complex (IgG-peroxidase).
    • To determine the binding constants and activation energies of the antibody-immunoenzyme complex interaction.
    • To evaluate the influence of immobilization methods on antibody-antigen binding.

    Summary:

    • Immobilized antibodies against human immunoglobulin G (IgG) were studied using an IgG-peroxidase (IgG-P) complex.

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  • Binding kinetics and dissociation revealed reversible interactions, similar to solution-phase antigen-antibody reactions.
  • Binding constants were high (up to 4.2 x 10^8 M-1), and immobilization method/carrier did not significantly impact binding rates.
  • Activation energies for binding were determined (7.3 and 4.1 kcal/mole for different immobilization strategies).

    • Impact:

    • Provides insights into the behavior of immobilized antibodies in biosensing applications.
    • Demonstrates the feasibility of using antigen-enzyme complexes for antibody titration.
    • Contributes to the development of more efficient and sensitive immunoassays.