Advanced

A glucose dehydrogenase biosensor as an additional signal amplification step in an enzyme-flow immunoassay.

Nistor, Catalin LU ; Rose, Andreas; Wollenberger, Ulla; Pfeiffer, Dorothea and Emnéus, Jenny LU (2002) In Analyst 127(8). p.1076-1081
Abstract
Both the antibody affinity and the detectability of the label are essential in deciding the final characteristics of a heterogeneous immunoassay. This paper describes an approach to obtain a supplementary enhancement of the signal generated by using an enzyme label, e.g., by including the product of the enzymatic reaction in an additional amplification cycle during the detection step performed with an amperometric biosensor based on glucose dehydrogenase (GDH). An immunoassay format with a labelled analyte derivative that competes with the analyte present in the sample for a limited amount of antibody binding sites was employed. The beta-galactosidase label hydrolyses the substrate aminophenyl-beta-galactopyranoside, and the generated... (More)
Both the antibody affinity and the detectability of the label are essential in deciding the final characteristics of a heterogeneous immunoassay. This paper describes an approach to obtain a supplementary enhancement of the signal generated by using an enzyme label, e.g., by including the product of the enzymatic reaction in an additional amplification cycle during the detection step performed with an amperometric biosensor based on glucose dehydrogenase (GDH). An immunoassay format with a labelled analyte derivative that competes with the analyte present in the sample for a limited amount of antibody binding sites was employed. The beta-galactosidase label hydrolyses the substrate aminophenyl-beta-galactopyranoside, and the generated aminophenol enters then into a bioelectrocatalytic amplification cycle at the GDH biosensor. The principle was applied for determination of 4-nitrophenol, with the best minimal concentration of 1.5 microM and a midpoint of the calibration of 24 microM. The potentials and limitations of such a system are discussed. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Analyst
volume
127
issue
8
pages
1076 - 1081
publisher
Royal Society of Chemistry
external identifiers
  • wos:000177201900012
  • pmid:12195949
  • scopus:0036679274
ISSN
1364-5528
DOI
10.1039/b203452b
language
English
LU publication?
yes
id
31e17f38-485f-4324-be67-f72cc473b767 (old id 110129)
date added to LUP
2007-06-27 13:45:10
date last changed
2017-08-27 05:40:20
@article{31e17f38-485f-4324-be67-f72cc473b767,
  abstract     = {Both the antibody affinity and the detectability of the label are essential in deciding the final characteristics of a heterogeneous immunoassay. This paper describes an approach to obtain a supplementary enhancement of the signal generated by using an enzyme label, e.g., by including the product of the enzymatic reaction in an additional amplification cycle during the detection step performed with an amperometric biosensor based on glucose dehydrogenase (GDH). An immunoassay format with a labelled analyte derivative that competes with the analyte present in the sample for a limited amount of antibody binding sites was employed. The beta-galactosidase label hydrolyses the substrate aminophenyl-beta-galactopyranoside, and the generated aminophenol enters then into a bioelectrocatalytic amplification cycle at the GDH biosensor. The principle was applied for determination of 4-nitrophenol, with the best minimal concentration of 1.5 microM and a midpoint of the calibration of 24 microM. The potentials and limitations of such a system are discussed.},
  author       = {Nistor, Catalin and Rose, Andreas and Wollenberger, Ulla and Pfeiffer, Dorothea and Emnéus, Jenny},
  issn         = {1364-5528},
  language     = {eng},
  number       = {8},
  pages        = {1076--1081},
  publisher    = {Royal Society of Chemistry},
  series       = {Analyst},
  title        = {A glucose dehydrogenase biosensor as an additional signal amplification step in an enzyme-flow immunoassay.},
  url          = {http://dx.doi.org/10.1039/b203452b},
  volume       = {127},
  year         = {2002},
}