Show simple item record

dc.creatorLazarević-Pašti, Tamara
dc.creatorVasić, Vesna M.
dc.date.accessioned2018-03-01T22:02:57Z
dc.date.available2018-03-01T22:02:57Z
dc.date.issued2011
dc.identifier.issn1311-5065
dc.identifier.urihttp://vinar.vin.bg.ac.rs/handle/123456789/4534
dc.description.abstractThe conversion of diazinon, the model compound for OPs, to more potent AChE inhibitor diazoxon was investigated, using enzyme myeloperoxidase (MPO) as an oxidant. The aim was to enhance its inhibitory power in order to develop rapid, effective and specific acethylcholinesterase (AChE)-based bioanalytical method for its detection in environment. 5-min incubation of 1 x 10(-5) M - 1 x 10(-7) M diazinon with 100 nM MPO increased the degree of AChE inhibition from 80 to 10% due to the formation of diazoxon, compared to the control values for samples containing the same diazinon concentrations in untreated samples. The calibration graph for diazinon detection with AChE assay after incubation with MPO was constructed. While the lower detection limit of diazinon (10% AChE inhibition) before oxidation was ca. 1 x 10(-5) M, the detection limit after oxidation was below 1 x 10(-8) M.en
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172023/RS//
dc.rightsrestrictedAccessen
dc.sourceJournal of Environmental Protection and Ecologyen
dc.subjectdiazinonen
dc.subjectmyeloperoxidaseen
dc.subjectoxidationen
dc.subjectbioanalyticsen
dc.subjectpesticidesen
dc.titleOxidation of Diazinon for the Sensitive Detection By Cholinesterase-Based Bioanalytical Methoden
dc.typearticleen
dcterms.abstractЛазаревић-Пасти Тамара; Васић Весна М;
dc.citation.volume12
dc.citation.issue3
dc.citation.spage1168
dc.citation.epage1173
dc.identifier.wos000296305700045
dc.citation.rankM23


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record