Purification of a phospholipase A(2) from Lonomia obliqua caterpillar bristle extract

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dc.contributor.authorSeibert, C. S.
dc.contributor.authorTanaka-Azevedo, A. M.
dc.contributor.authorSantoro, M. L.
dc.contributor.authorMackessy, S. P.
dc.contributor.authorTorquato, RJS
dc.contributor.authorLebrun, I
dc.contributor.authorTanaka, A. S.
dc.contributor.authorSano-Martins, I. S.
dc.contributor.institutionInst Butanan
dc.contributor.institutionUniv No Colorado
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:41:07Z
dc.date.available2016-01-24T12:41:07Z
dc.date.issued2006-04-21
dc.description.abstractLonomia obliqua caterpillar bristle extract induces both direct and indirect hemolytic activity on human and rat washed erythrocytes, and provokes intravascular hemolysis in Wistar rats. Indirect hemolytic activity is assumed to be caused by a phospholipase A(2) (PLA(2)) present in this extract, and this investigation was initiated in order to characterize this enzyme. Phospholipase A, activity of crude extract was inhibited by both a PLA(2)-specific inhibitor (pBpb) and the metal ion chelator EDTA. L. obliqua PLA(2) was purified by liquid chromatography from the crude bristle extract and had a molecular mass of 15 kDa and a pI of 5.9: its N-terminal sequence showed high homology to a sequence of a putative PLA(2) obtained from a cDNA library of L. obliqua bristles, and it is tentatively placed among Group III phospholipases A(2). This enzyme was stable at 4 degrees C sensitive to higher temperatures, and its maximum catalytic activity was at pH 8.0. L. obliqua PLA(2) induced hemolysis only when incubated with exogenous lecithin. Thus, the PLA(2) purified herein appears to be responsible for the indirect hemolytic activity of the crude bristle extract. (c) 2006 Elsevier Inc. All rights reserved.en
dc.description.affiliationInst Butanan, Lab Fisiopatol, São Paulo, Brazil
dc.description.affiliationUniv No Colorado, Sch Biol Sci, Greeley, CO 80639 USA
dc.description.affiliationUNIFESP, Dept Bioquim, São Paulo, Brazil
dc.description.affiliationInst Butanan, Lab Bioquim & Biofis, São Paulo, Brazil
dc.description.affiliationUnifespUNIFESP, Dept Bioquim, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent1027-1033
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2006.02.071
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 342, n. 4, p. 1027-1033, 2006.
dc.identifier.doi10.1016/j.bbrc.2006.02.071
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/28851
dc.identifier.wosWOS:000236316100004
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectLonomia obliquaen
dc.subjectphospholipase A(2)en
dc.subjectindirect hemolysisen
dc.subjecterythrocytesen
dc.subjectintravascular hemolysisen
dc.subjectcaterpillaren
dc.subjectlecithinen
dc.subjectchromatographyen
dc.titlePurification of a phospholipase A(2) from Lonomia obliqua caterpillar bristle extracten
dc.typeArtigo
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