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Evaluation of acetylcholinesterase source from fish, Tor tambroides for detection of carbamate

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dc.Chemicals/CASacetylcholinesterase, 9000-81-1; ubiquitin protein ligase, 134549-57-8; Acetylcholinesterase; BRAP protein, human; Carbamates; Insecticides; Ubiquitin-Protein Ligases; Water Pollutants, Chemical
dc.citedby6
dc.contributor.affiliationsFaculty of Medicine and Health Sciences
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.affiliationsUniversiti Malaysia Sabah (UMS)
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.affiliationsUniversiti Kebangsaan Malaysia (UKM)
dc.contributor.authorAhmad S.A.en_US
dc.contributor.authorSabullah M.K.en_US
dc.contributor.authorShamaan N.A.en_US
dc.contributor.authorShukor M.Y.A.en_US
dc.contributor.authorJirangon H.en_US
dc.contributor.authorKhalid A.en_US
dc.contributor.authorSyed M.A.en_US
dc.date.accessioned2024-05-29T01:57:06Z
dc.date.available2024-05-29T01:57:06Z
dc.date.issued2016
dc.description.abstractAcetylcholinesterase (AChE) from the brain tissue of local freshwater fish, Tor tambroides was isolated through affinity purification. Acetylthiocholine iodide (ATCi) was preferable synthetic substrate to purified AChE with highest maximal velocity (Vmax) and lowest biomolecular constant (Km) at 113.60 Umg-1 and 0.0689 mM, respectively, with highest catalytic efficiency ratio (Vmax/Km) of 1648.77. The optimum pH was 7.5 with sodium phosphate buffer as medium, while optimal temperature was in the range of 25 to 35�C. Bendiocarp, carbofuran, carbaryl, methomyl and propoxur significantly lowered the AChE activity greater than 50%, and the IC50 value was estimated at inhibitor concentration of 0.0758, 0.0643, 0.0555, 0.0817 and 0.0538 ppm, respectively. � Triveni Enterprises.en_US
dc.description.natureFinalen_US
dc.identifier.CODENJEBID
dc.identifier.epage484
dc.identifier.issn2548704
dc.identifier.issue4
dc.identifier.pmid27498490
dc.identifier.scopus2-s2.0-84984863531
dc.identifier.spage479
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84984863531&partnerID=40&md5=08f3ed9659e5024572f716076fa62a20
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/9900
dc.identifier.volume37
dc.languageEnglish
dc.language.isoen_USen_US
dc.publisherTriveni Enterprisesen_US
dc.relation.ispartofJournal of Environmental Biology
dc.sourceScopus
dc.subjectAcetylcholinesteraseen_US
dc.subjectBrainen_US
dc.subjectCarbamateen_US
dc.subjectOrganophosphateen_US
dc.subjectTor tambroidesen_US
dc.titleEvaluation of acetylcholinesterase source from fish, Tor tambroides for detection of carbamateen_US
dc.title.alternativeJ. Environ. Biol.en_US
dc.typeArticleen_US
dspace.entity.typePublication

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