title: Immunochemistry at interfaces.
abstract: The immunochemistry of antibody binding to solid-phase immobilized antigen is reviewed. Experimental data are compared with different theoretical models of reaction mechanisms at solid-liquid interfaces. It was found that reactions at the solid-liquid interface can become limited by the diffusion rate due to depletion of reactants close to the surface, even though the intrinsic bimolecular reaction at the surface is reaction-rate limited. The forward reaction-rate constant decreases with increasing concentration of bound antibodies at the surface, and when not limited by diffusion the forward reaction rate can be more than 1000-fold slower than the corresponding reaction in a liquid solution. Possible explanations for this phenomenon are discussed. The dissociation of bound antibodies is a slow process at solid phases. The antigen-antibody complexes formed are practically irreversible. Some evidence is presented which indicates that the stability of these complexes can be due to attractive lateral interactions between bound antibodies.
authors.affiliation: Department of Histology, University of Göteborg.
authors.forename: H
authors.initials: H
authors.lastname: Nygren
authors.forename: M
authors.initials: M
authors.lastname: Stenberg
mesh_terms: D000937:Antigen-Antibody Reactions; D000954:Antigens, Surface; D007120:Immunochemistry; D007700:Kinetics
chemical_list: D000954:Antigens, Surface