An amperometric biosensor, based on an anti-7-hydroxycoumarin (7-OH-coumarin) antibody immobilized at the surface of a glassy carbon electrode, and contained behind a cellulose dialysis membrane, is described. The electrochemical behaviour of this metabolite at the bare glassy carbon electrode was found to be well defined by using differential-pulse voltammetry, and a 90% decrease in peak height was observed on binding of the antibody to the antigen, which occurs at the electroactive site of 7-OH-coumarin. The kinetics of the antibody-antigen reaction was investigated and a first-order reaction was observed with k = 0.0329 mA min-1. This system provides a novel method for studying antibody specificity and the kinetics of such antibody-antigen interactions.
%0 Journal Article
%1 citeulike:700744
%A Dempsey, E.
%A O'Sullivan, C.
%A Smyth, M. R.
%A Egan, D.
%A O'Kennedy, R.
%A Wang, J.
%C School of Chemical Sciences, Dublin City University, Ireland.
%D 1993
%J Analyst
%K amperometry antibody electrochemistry immunoelectrode
%N 4
%P 411--413
%T Development of an antibody-based amperometric biosensor to study the reaction of 7-hydroxycoumarin with its specific antibody.
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8494174
%V 118
%X An amperometric biosensor, based on an anti-7-hydroxycoumarin (7-OH-coumarin) antibody immobilized at the surface of a glassy carbon electrode, and contained behind a cellulose dialysis membrane, is described. The electrochemical behaviour of this metabolite at the bare glassy carbon electrode was found to be well defined by using differential-pulse voltammetry, and a 90% decrease in peak height was observed on binding of the antibody to the antigen, which occurs at the electroactive site of 7-OH-coumarin. The kinetics of the antibody-antigen reaction was investigated and a first-order reaction was observed with k = 0.0329 mA min-1. This system provides a novel method for studying antibody specificity and the kinetics of such antibody-antigen interactions.
@article{citeulike:700744,
abstract = {An amperometric biosensor, based on an anti-7-hydroxycoumarin (7-OH-coumarin) antibody immobilized at the surface of a glassy carbon electrode, and contained behind a cellulose dialysis membrane, is described. The electrochemical behaviour of this metabolite at the bare glassy carbon electrode was found to be well defined by using differential-pulse voltammetry, and a 90% decrease in peak height was observed on binding of the antibody to the antigen, which occurs at the electroactive site of 7-OH-coumarin. The kinetics of the antibody-antigen reaction was investigated and a first-order reaction was observed with k = 0.0329 mA min-1. This system provides a novel method for studying antibody specificity and the kinetics of such antibody-antigen interactions.},
added-at = {2007-11-03T00:18:07.000+0100},
address = {School of Chemical Sciences, Dublin City University, Ireland.},
author = {Dempsey, E. and O'Sullivan, C. and Smyth, M. R. and Egan, D. and O'Kennedy, R. and Wang, J.},
biburl = {https://www.bibsonomy.org/bibtex/28d351573438813ae5312de4c9c311e0a/bsmyth},
citeulike-article-id = {700744},
description = {my barry smyth},
interhash = {94ac8d257f9e3635419be83f9ccbc2ea},
intrahash = {8d351573438813ae5312de4c9c311e0a},
issn = {0003-2654},
journal = {Analyst},
keywords = {amperometry antibody electrochemistry immunoelectrode},
month = {April},
number = 4,
pages = {411--413},
priority = {2},
timestamp = {2007-11-03T00:18:13.000+0100},
title = {Development of an antibody-based amperometric biosensor to study the reaction of 7-hydroxycoumarin with its specific antibody.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=8494174},
volume = 118,
year = 1993
}