Selective activity of butyrylcholinesterase in serum by a chemiluminescent assay

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dc.contributor.authorYavo, B.
dc.contributor.authorBrunetti, Iguatemy Lourenço [UNESP]
dc.contributor.authorFonseca, Luiz Marcos da [UNESP]
dc.contributor.authorCatalani, L. H.
dc.contributor.authorCampa, A.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:24:32Z
dc.date.available2014-05-20T13:24:32Z
dc.date.issued2001-09-01
dc.description.abstractIn a previous study, we showed that purified commercial esterase activity can be detected in a chemiluminescent assay based on the hydrolysis of 2-methyl-1-propenylbenzoate (MPB) to 2-methyl-1-propenol, which is subsequently oxidized by the horseradish peroxidase (HRP)-H2O2 system. The purpose of this study was to verify the applicability of this assay to human serum. The existence of an esterase activity capable of hydrolysing MPB is indicated by the fact that the MPB-scruin-HRP-H2O2 System consumes oxygen and emits light. Both signals were abolished by prior serum heat inactivation and were preserved when serum was stored at less than or equal to4 degreesC. Addition of aliesterase inhibitors, such as fluoride ion and trichlorfon or the cholinesterase inhibitor eserine, totally prevents light emission. The butyrylcholinesterase-specific substrate benzoylcholine causes a delay in both O-2 uptake and light emission, while the specific acetylcholinesterase substrate, acetyl-beta -methylcholine, had practically no effect. Purified butyrylcholinesterase, but not acetylcholinesterase, triggered light emission. The finding that butyryleholinesterase is responsible for the hydrolysis of MPB in serum should serve as the basis for the development of a specific chemiluminescent assay for this enzyme. Copyright (C) 2001 John Wiley & Sons, Ltd.en
dc.description.affiliationUniv São Paulo, Fac Ciências Farmaceut, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniv Estadual Paulista, Fac Ciências Farmaceut, BR-14801902 Araraquara, Brazil
dc.description.affiliationUniv São Paulo, Inst Quim, BR-05599970 São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciências Farmaceut, BR-14801902 Araraquara, Brazil
dc.format.extent299-304
dc.identifierhttp://dx.doi.org/10.1002/bio.658
dc.identifier.citationLuminescence. W Sussex: John Wiley & Sons Ltd, v. 16, n. 5, p. 299-304, 2001.
dc.identifier.doi10.1002/bio.658
dc.identifier.issn1522-7235
dc.identifier.lattes4419635633356792
dc.identifier.urihttp://hdl.handle.net/11449/7640
dc.identifier.wosWOS:000171848100001
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofLuminescence
dc.relation.ispartofjcr1.671
dc.relation.ispartofsjr0,396
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectesterasept
dc.subjectbutyrylcholinesterasept
dc.subjectpseudocholinesterasept
dc.subjecthorseradish peroxidasept
dc.subjectchemiluminescencept
dc.titleSelective activity of butyrylcholinesterase in serum by a chemiluminescent assayen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-Blackwell
unesp.author.lattes4419635633356792
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt

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