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

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dc.contributor.authorAhmad, SAen_US
dc.contributor.authorSabullah, MKen_US
dc.contributor.authorShamaan, NAen_US
dc.contributor.authorAbd Shukor, MYen_US
dc.contributor.authorJirangon, Hen_US
dc.contributor.authorKhalid, Aen_US
dc.contributor.authorSyed, MAen_US
dc.date.accessioned2024-05-29T03:25:14Z
dc.date.available2024-05-29T03:25:14Z
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 (V-max) and lowest biomolecular constant (K-m) at 113.60 Umg(-1) and 0.0689 mM, respectively, with highest catalytic efficiency ratio (V-max/K-m) of 1648.77. The optimum p11 was 7.5 with sodium phosphate butler as medium, while optimal temperature was in the range of 25 to 35 degrees C. Bendiocarp, carbofuran, carbaryl, methomyl and propoxur significantly lowered the AChE activity greater than 50%, and the IC50 value kvas estimated at inhibitor concentration of 0.0758, 0.0643, 0.0555, 0.0817 and 0.0538 ppm, respectively.
dc.identifier.epage484
dc.identifier.issn0254-8704
dc.identifier.issue4
dc.identifier.scopusWOS:000382473800001
dc.identifier.spage479
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/11918
dc.identifier.volume37
dc.languageEnglish
dc.language.isoen_US
dc.publisherTriveni Enterprisesen_US
dc.relation.ispartofJournal Of Environmental Biology
dc.sourceWeb Of Science (ISI)
dc.subjectAcetylcholinesterase; Brain; Carbainate; Organophosphate; Tor tamhroidesen_US
dc.titleEvaluation of acetylcholinesterase source from fish, Tor tambroides for detection of carbaiiiate
dc.typeArticleen_US
dspace.entity.typePublication

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