Development of a one-step strip for the detection of triazophos residues in environmental samples

Gui, Wenjun; Wang, Zhen; Guo, Yirong; Zhu, Guonian

doi:10.1016/j.ab.2008.03.013

Cited by 57 publications

(26 citation statements)

References 15 publications

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“…6 The effect of different volumes of gold-labeled antibody for developing IC test strip: a 1 μl of nanogold-labeled antibody was used; b 0.7 μl of nanogold-labeled antibody was used; c 0.5 μl nanogoldlabeled antibody was used particles smaller than 15 nm were found to be too small to produce a strength color. Furthermore, colloidal gold particles larger than 60-70 nm offered a self-aggregation after the particles had been stored at 4°C for several days [19,21]. For conjugation, immunoglobulin is directly absorbed on particle surfaces and this process can be accomplished by non-covalent reactions including London-van der Waals force and hydrophobic interactions.…”

Section: Discussionmentioning

confidence: 99%

Colloidal Nanogold-Based Immunochromatographic Strip Test for the Detection of Digoxin Toxicity

Omidfar

Kia

Kashanian

et al. 2009

Appl Biochem Biotechnol

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Digoxin is widely used as a cardiac glycoside drug in the treatment of various heart conditions. Because it is a toxic drug, it should be regularly monitored in the serum of patients under treatment. In this study, colloidal nanogold is synthesized and the preparation of nanogold-labeled monoclonal antibody probe to digoxin is described under optimal conditions. In addition, an immunochromatographic (IC) method for digoxin analysis employing nanogold-labeled probe is developed. With this technique, it requires only 5 min to complete the quantitative detection of digoxin. The detection time is decreased 20-30 times in comparison to radioimmunoassay (RIA). The sensitivity to digoxin was about 2 ng/ml by naked eye, which is within the therapeutic and toxic ranges of digoxin. The results of serum samples obtained by IC strip were in agreement with those obtained by RIA. The IC strip was sufficiently sensitive and accurate to be used for the rapid detection of digoxin in serum samples.

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Section: Discussionmentioning

confidence: 99%

Colloidal Nanogold-Based Immunochromatographic Strip Test for the Detection of Digoxin Toxicity

Omidfar

Kia

Kashanian

et al. 2009

Appl Biochem Biotechnol

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“…1 Due to its relative stability, widespread use and long half-life, residues of triazophos in agricultural products and the natural environment may result in potential hazards to human health and animals. 2 Since the end of 2016, triazophos has been banned for use on vegetables by the Chinese Ministry of Agriculture, but the illegal use of triazophos for vegetables and fruits still happens now and then. Therefore, it is important to develop a highly sensitive and selective method for the detection of triazophos residues in agricultural and environmental samples.…”

Section: Introductionmentioning

confidence: 99%

Biomimetic enzyme-linked immunoassay based on a molecularly imprinted 96-well plate for the determination of triazophos residues in real samples

et al. 2018

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In this study, a direct competitive biomimetic enzyme-linked immune-sorbent assay (BELISA) based on a molecularly imprinted nanomembrane as an artificial antibody was developed for the determination of triazophos in real samples. The imprinted film was directly synthesized on the well surface of a 96-well plate using a dummy molecular template under the conditions of thermal polymerization. The developed BELISA using a hapten of triazophos as an enzyme-labeled probe is much more sensitive, simple, quick, steady and inexpensive than the other instrumental and immuno assay methods. Under optimal conditions, the linear range of the method was 0.001-10 000 mg L À1 with a good regression coefficient of 0.977. The sensitivity (IC 50 ) and the limit of detection (LOD) of BELISA were 428 mg L À1 and 0.001 mg L À1, respectively. This method was performed to detect triazophos in cabbage and apple samples, and showed excellent recovery and relative standard deviations (RSDs) ranging from 70.5 to 119.8% and from 5.2 to 19.7%, respectively. The results correlated well with those obtained using high performance liquid chromatography-tandem mass spectrometry.

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“…Enzymatic activities for parathion and methyl parathion were measured using a spectrophotometer to monitor the production of p-nitrophenol at 405 nm (Dumas et al 1989). Isofenphos-methyl, isocarbophos, isofenphos, triazophos, profenofos, butamifos, and phosalone were analyzed by high-performance liquid chromatography (HPLC) (Ettan LC; Amersham Biosciences, Uppsala, Sweden) and detected by a UV-900 detector at 245 nm (Li et al 2009;Yang et al 2011;Li et al 2011;Gui et al 2008;Jonsson et al 2001;Sanchez et al 2004). Fenitrothion, phoxim, and methidathion were detected at 270 nm (Hong et al 2007;Shen et al 2010), and chlorpyrifos was detected at 230 nm ).…”

Section: Effect Of Metal Ions and Chemical Agents On Imh Activitymentioning

confidence: 99%

An isofenphos-methyl hydrolase (Imh) capable of hydrolyzing the P–O–Z moiety of organophosphorus pesticides containing an aryl or heterocyclic group

Liu

Zhang

et al. 2011

Appl Microbiol Biotechnol

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Organophosphorus pesticide (OP) hydrolases play key roles in the degradation and decontamination of agricultural and household OPs and in the detoxification of chemical warfare agents. In this study, an isofenphos-methyl hydrolase gene (imh) was cloned from the isocarbophos-degrading strain of Arthrobacter sp. scl-2 using the polymerase chain reaction method. Isofenphos-methyl hydrolase (Imh) showed 98% sequence identity with the isofenphos hydrolase from Arthrobacter sp. strain B-5. Imh was highly expressed in Escherichia coli BL21 (DE3), and the His(6)-tagged Imh was purified (1.7 mg/ml) with a specific activity of 14.35 U/mg for the substrate isofenphos-methyl. The molecular mass of the denatured Imh is about 44 kDa, and the isoelectric point (pI) value was estimated to be 3.4. The optimal pH and temperature for hydrolysis of isofenphos-methyl were pH 8.0 and 35 °C, respectively. The secondary structure of Imh shows that Imh is a metallo-dependent hydrolase, and it was found that Imh was completely inhibited by the metalloprotease inhibitor 1,10-phenanthroline (0.5 mM), and the catalytic activity was restored by the subsequent addition of Zn(2+). Interestingly, Imh had a relatively broader substrate specificity and was capable of hydrolyzing 12 of the tested oxon and thion OPs with the P-O-Z moiety instead of the P-S(C)-Z moiety. Furthermore, it was found that the existence of an aryl or heterocyclic group in the leaving group (Z) is also important in determining the substrate specificity. Among all the substrates hydrolyzed by Imh, it was assumed that Imh preferred P-O-Z substrates still with a phosphamide bond (P-N), such as isofenphos-methyl, isofenphos, isocarbophos, and butamifos. The newly characterized Imh has a great potential for use in the decontamination and detoxification of agricultural and household OPs and is a good candidate for the study of the catalytic mechanism and substrate specificity of OP hydrolases.

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Development of a one-step strip for the detection of triazophos residues in environmental samples

Cited by 57 publications

References 15 publications

Colloidal Nanogold-Based Immunochromatographic Strip Test for the Detection of Digoxin Toxicity

Colloidal Nanogold-Based Immunochromatographic Strip Test for the Detection of Digoxin Toxicity

Biomimetic enzyme-linked immunoassay based on a molecularly imprinted 96-well plate for the determination of triazophos residues in real samples

An isofenphos-methyl hydrolase (Imh) capable of hydrolyzing the P–O–Z moiety of organophosphorus pesticides containing an aryl or heterocyclic group

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