Abstract
As a consequence of organophosphorus (OP) toxins posing a threat to human life globally, organophosphorus hydrolase (OPH) has become the enzyme of choice to detoxify such compounds. Organophosphorus hydrolase was covalently immobilized onto a quartz substrate for utilization in paraoxon detection. The substrate was cleaned and modified prior to chemical attachment. Each modification step was monitored by imaging ellipsometry as the thickness increased with each modification step. The chemically attached OPH was labeled with a fluorescent dye (7-isothiocyanato-4-methylcoumarin) for the detection of paraoxon in aqueous solution, ranging from 10-9 to 10-5 M. UV-visible spectra were also acquired for the determination of the hydrolysis product of paraoxon, namely p-nitrophenol.
| Original language | English |
|---|---|
| Pages (from-to) | 7016-7021 |
| Number of pages | 6 |
| Journal | Analytical Chemistry |
| Volume | 78 |
| Issue number | 19 |
| DOIs | |
| State | Published - Oct 1 2006 |
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ASJC Scopus subject areas
- Analytical Chemistry
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Detection of organophosphorus compounds by covalently immobilized organophosphorus hydrolase. / Orbulescu, Jhony; Constantine, Celeste A.; Rastogi, Vipin K.; Shah, Saumil S.; DeFrank, Joseph J.; Leblanc, Roger.
In: Analytical Chemistry, Vol. 78, No. 19, 01.10.2006, p. 7016-7021.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Detection of organophosphorus compounds by covalently immobilized organophosphorus hydrolase
AU - Orbulescu, Jhony
AU - Constantine, Celeste A.
AU - Rastogi, Vipin K.
AU - Shah, Saumil S.
AU - DeFrank, Joseph J.
AU - Leblanc, Roger
PY - 2006/10/1
Y1 - 2006/10/1
N2 - As a consequence of organophosphorus (OP) toxins posing a threat to human life globally, organophosphorus hydrolase (OPH) has become the enzyme of choice to detoxify such compounds. Organophosphorus hydrolase was covalently immobilized onto a quartz substrate for utilization in paraoxon detection. The substrate was cleaned and modified prior to chemical attachment. Each modification step was monitored by imaging ellipsometry as the thickness increased with each modification step. The chemically attached OPH was labeled with a fluorescent dye (7-isothiocyanato-4-methylcoumarin) for the detection of paraoxon in aqueous solution, ranging from 10-9 to 10-5 M. UV-visible spectra were also acquired for the determination of the hydrolysis product of paraoxon, namely p-nitrophenol.
AB - As a consequence of organophosphorus (OP) toxins posing a threat to human life globally, organophosphorus hydrolase (OPH) has become the enzyme of choice to detoxify such compounds. Organophosphorus hydrolase was covalently immobilized onto a quartz substrate for utilization in paraoxon detection. The substrate was cleaned and modified prior to chemical attachment. Each modification step was monitored by imaging ellipsometry as the thickness increased with each modification step. The chemically attached OPH was labeled with a fluorescent dye (7-isothiocyanato-4-methylcoumarin) for the detection of paraoxon in aqueous solution, ranging from 10-9 to 10-5 M. UV-visible spectra were also acquired for the determination of the hydrolysis product of paraoxon, namely p-nitrophenol.
UR - http://www.scopus.com/inward/record.url?scp=33749459214&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33749459214&partnerID=8YFLogxK
U2 - 10.1021/ac061118m
DO - 10.1021/ac061118m
M3 - Article
C2 - 17007528
AN - SCOPUS:33749459214
VL - 78
SP - 7016
EP - 7021
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 19
ER -