A glucose dehydrogenase biosensor as an additional signal amplification step in an enzyme-flow immunoassay.
(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:
https://lup.lub.lu.se/record/110129
- author
- Nistor, Catalin LU ; Rose, Andreas ; Wollenberger, Ulla ; Pfeiffer, Dorothea and Emnéus, Jenny LU
- organization
- publishing date
- 2002
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 31e17f38-485f-4324-be67-f72cc473b767 (old id 110129)
- date added to LUP
- 2016-04-01 17:12:14
- date last changed
- 2024-07-02 13:21:06
@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}}, doi = {{10.1039/b203452b}}, volume = {{127}}, year = {{2002}}, }