%0 Journal Article %1 citeulike:485973 %A Nygren, H. %A Stenberg, M. %C Department of Histology, University of Göteborg. %D 1989 %J Immunology %K methodology immunoassay statistic antibody review %N 3 %P 321--327 %T Immunochemistry at interfaces. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2649437 %V 66 %X 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.

@article{citeulike:485973, 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.}, added-at = {2006-07-07T01:10:50.000+0200}, address = {Department of Histology, University of Göteborg.}, author = {Nygren, H. and Stenberg, M.}, biburl = {https://www.bibsonomy.org/bibtex/2782529e9a465eed9ea4b8a32781c5c3a/biblio24}, citeulike-article-id = {485973}, interhash = {c32fd7ded56b7d33122fa11764321cc9}, intrahash = {782529e9a465eed9ea4b8a32781c5c3a}, issn = {0019-2805}, journal = {Immunology}, keywords = {methodology immunoassay statistic antibody review}, month = {March}, number = 3, pages = {321--327}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Immunochemistry at interfaces.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=2649437}, volume = 66, year = 1989 }