%0 Journal Article %1 citeulike:574193 %A Rabbany, S. Y. %A Piervincenzi, R. T. %A Kusterbeck, A. W. %A Bredehorst, R. %A Ligler, Fs %C HOFSTRA UNIV,BIOENGN PROGRAM,104 WEED HALL HEMPSTEAD NY 11550 USN,RES LAB,CTR BIOMOL SCI & ENGN WASHINGTON DC 20375 UNIV HAMBURG,DEPT BIOCHEM & MOL BIOL D-20146 HAMBURG GERMANY %D 1998 %J Analytical letters %K displacement fia methodology immunoassay %N 10 %P 1663--1675 %T Dissociation rate kinetics in a solid-phase flow immunoassay %V 31 %X Solid-phase displacement assays allow extremely fast analyses when performed under continuous flow conditions. Continuous dissociation of labeled antigen from the immobilized saturated antibodies occurs even in the absence of competing unlabeled antigen. This spontaneous dissociation creates more unoccupied antibody binding sites which affect the magnitude of the signal generated. In order to evaluate the impact of this phenomenon in more detail, we extended the law of mass action to solid-phase binding assays and analyzed the dissociation kinetics of labeled antigen under continuous flow conditions. The effect of the nowon the dissociation kinetics was determined by calculation of the apparent dissociation rate constants (k(d)) which increase with an increase in the now rate. These dissociation rate constants are approximately 20- to 30-fold lower than those obtained from displacement studies (i.e., in the presence of competing unlabeled antigen). The difference in the dissociation rate constants obtained in the two studies is mostlikely a function of the degree of reassociation. The results of thisstudy provide a basis for better understanding antibody kinetics at solid-liquid interfaces under flow conditions.

@article{citeulike:574193, abstract = {Solid-phase displacement assays allow extremely fast analyses when performed under continuous flow conditions. Continuous dissociation of labeled antigen from the immobilized saturated antibodies occurs even in the absence of competing unlabeled antigen. This spontaneous dissociation creates more unoccupied antibody binding sites which affect the magnitude of the signal generated. In order to evaluate the impact of this phenomenon in more detail, we extended the law of mass action to solid-phase binding assays and analyzed the dissociation kinetics of labeled antigen under continuous flow conditions. The effect of the nowon the dissociation kinetics was determined by calculation of the apparent dissociation rate constants (k(d)) which increase with an increase in the now rate. These dissociation rate constants are approximately 20- to 30-fold lower than those obtained from displacement studies (i.e., in the presence of competing unlabeled antigen). The difference in the dissociation rate constants obtained in the two studies is mostlikely a function of the degree of reassociation. The results of thisstudy provide a basis for better understanding antibody kinetics at solid-liquid interfaces under flow conditions.}, added-at = {2006-07-07T01:10:50.000+0200}, address = {HOFSTRA UNIV,BIOENGN PROGRAM,104 WEED HALL HEMPSTEAD NY 11550 USN,RES LAB,CTR BIOMOL SCI \& ENGN WASHINGTON DC 20375 UNIV HAMBURG,DEPT BIOCHEM \& MOL BIOL D-20146 HAMBURG GERMANY}, author = {Rabbany, S. Y. and Piervincenzi, R. T. and Kusterbeck, A. W. and Bredehorst, R. and Ligler, Fs}, biburl = {https://www.bibsonomy.org/bibtex/21df2a6f0d47f36aa52dd05d994f1c75a/biblio24}, citeulike-article-id = {574193}, interhash = {7660761d357175faf6dc543f8187debe}, intrahash = {1df2a6f0d47f36aa52dd05d994f1c75a}, journal = {Analytical letters}, keywords = {displacement fia methodology immunoassay}, number = 10, pages = {1663--1675}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Dissociation rate kinetics in a solid-phase flow immunoassay}, volume = 31, year = 1998 }