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.
%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
}