Evidence map›Paper›PMID 40900406›Full record

ArticleApplied biochemistry and biotechnology2025

Investigation of Biopesticides for the Pest Control Through Inhibition of the Acetylcholinesterase Purified from Loxostege sticticalis (L.) (Lepidoptera: Crambidae).

Demet Kızıl

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Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Demet KızılBursa Technical University Central Research Laboratory, 16310, Bursa, Türkiye. demet.kizil@btu.edu.tr.ORCID http://orcid.org/0000-0002-2346-7514

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylcholinesterase (AChE) is a cholinergic enzyme called acetylcholine acetylhydrolase. Acetylcholinesterase inhibition is one of the prominent methods in studies on pest control management. In this study, AChE was purified 103.7-fold from Loxostege sticticalis (L.) using an Edrophonium-Sepharose 6B affinity column, and some kinetic properties were investigated. The molecular weight of the purified enzyme was determined by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). Inhibition studies of AChE were realized with tacrine, edrophonium chloride, and cypermethrin, which are known inhibitors of AChE, as well as aqueous extracts of certain plant leaves. The subunit molecular weight of purified AChE was estimated to be approximately 56 kDa by SDS-PAGE analysis. The maximum activity of Loxostege sticticalis AChE was specified at 40.0 °C and pH 8.0. V

Indexed as

AcetylcholinesteraseBiological Control AgentsCholinesterase InhibitorsLepidopteraAnimalsKineticsPlant ExtractsPlant LeavesAcetylcholinesteraseBiological Control AgentsCholinesterase InhibitorsPlant ExtractsAcetylcholinesteraseBiopesticideInhibitionLoxostege sticticalis (L.)Pest management

Identifiers

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Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.