Antigen‐Antibody Interaction, Antibody Affinity, and Dissociation of Immune Complexes

Association of antibody with antigen depends on noncovalent interaction between the antibody-binding sites and the antigen. The magnitude of the binding energy depends on the degree of fit between the antigen and the binding site of the antibody, and this is termed the affinity of the antibody for that antigen. The term ‘affinity’ generally refers to a single antibody site for an antigenetically homogeneous molecule (e.g. hapten). Proteins contain several antigen determinants and the term ‘avidity’ is often used to characterize the antigen binding of the heterogeneous antibodies induced by such molecules. The average affinity (avidity) of antibodies is a significant aspect of most imrnunochemical techniques. Immunoassays of antigens make use of high-affinity antibodies. This is particularly important in radioimmunoassay, where the sensitivity of the test depends mainly on the affinity of the antibodies used (18). Antibodies of low affinity are better for purifying antigens (30). This is because lowaffinity antibody allows dissociation of the antibody-antigen complex under relatively mild conditions. No significant changes occur in avidity when antibodies are coupled to an insoluble matrix (39).

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