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The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution.

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dc.contributor.authorMontenegro Arce, María Fernanda
dc.contributor.authorMoral Naranjo, M. T.
dc.contributor.authorPáez de la Cadena, M.
dc.contributor.authorMuñoz Delgado, Encarnación
dc.contributor.authorVidal, C. J.
dc.contributor.authorCampoy Menéndez, Francisco Javier
dc.contributor.departmentBioquímica y Biología Molecular A
dc.date.accessioned2026-02-23T11:58:57Z
dc.date.available2026-02-23T11:58:57Z
dc.date.copyright© 2008 Elsevier Ireland Ltd.
dc.date.issued2008-09-25
dc.description.abstractButyrylcholinesterase (BuChE) and acetylcholinesterase (AChE) display both esterase and aryl acylamidase (AAA) activities. Their AAA activity can be measured using o-nitroacetanilide (ONA). In human samples depleted of acetylcholinesterase, we noticed that the ratio of amidase to esterase activities varied depending on the source, despite both activities being due to BuChE. Searching for an explanation, we compared the activities of BuChE molecular forms in samples of human colon, kidney and serum, and observed that BuChE monomers (G1) hydrolyzed o-nitroacetanilide much faster than tetramers (G4). This fact suggested that association might cause differences in the AAA site between single and polymerized subunits. This and other post-translational modifications in BuChE subunits probably determine their level of AAA activity. The higher amidase activity of monomers could justify the presence of single BuChE subunits in cells as a way to preserve the AAA activity of BuChE, which could be lost by oligomerization.
dc.formatapplication/pdf
dc.format.extent10
dc.identifier.citationChemico-Biological Interactions, Volume 175, Issues 1–3, 25 September 2008, Pages 336-339
dc.identifier.doihttps://doi.org/10.1016/j.cbi.2008.03.007
dc.identifier.eissn1872-7786
dc.identifier.issn0009-2797
dc.identifier.urihttp://hdl.handle.net/10201/210562
dc.languageeng
dc.publisherElsevier
dc.relationInstituto de Salud Carlos III, Spain (FIS-PI04-1504) and the Fundación Séneca de la Comunidad Autónoma de Murcia (00636/PI/04).
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0009279708001609
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectAryl acylamidase
dc.subjectBlood serum
dc.subjectMolecular forms
dc.subjectButyrylcholinesterase
dc.subject.odsNo relacionado con ningún objetivo de desarrollo sostenible
dc.titleThe level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution.
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/acceptedVersion
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relation.isAuthorOfPublication.latestForDiscovery2d4e44e6-9dda-4146-8aef-fe0c6b5a8b8f
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