Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom

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dc.contributor.authorToyama M.H.
dc.contributor.authorToyama D.D.O.
dc.contributor.authorPassero L.F.D.
dc.contributor.authorLaurenti M.D.
dc.contributor.authorCorbett C.E.
dc.contributor.authorTomokane T.Y.
dc.contributor.authorFonseca F.V.
dc.contributor.authorAntunes E.
dc.contributor.authorJoazeiro P.P.
dc.contributor.authorBeriam L.O.S.
dc.contributor.authorMartins M.A.C.
dc.contributor.authorMonteiro H.S.A.
dc.contributor.authorFonteles M.C.
dc.date.accessioned2024-03-13T01:43:20Z
dc.date.available2024-03-13T01:43:20Z
dc.date.issued2006
dc.description.abstractA novel L-amino acid oxidase (LAO) (Casca LAO) from Crotalus durissus cascavella venom was purified to a high degree of molecular homogeneity using a combination of molecular exclusion and ion-exchange chromatography system. The purified monomer of LAO presented a molecular mass of 68 kDa and pI estimated in 5.43, which were determined by two-dimensional electrophoresis. The 71st N-terminal amino acid sequence of the LAO from Crotalus durissus cascavella presented a high amino acid sequence similarities with other LAOs from Colloselasma rhosostoma, Crotalus adamanteus, Agkistrodon h. blomhoffi, Agkistrodon h. halys and Trimeresurus stejnegeri. LAO displayed a Michaelis-Menten behavior with a kilometer of 46.7 μM and an optimum pH for enzymatic activity of 6.5. Casca LAO induced a dose-dependent platelet aggregation, which was abolished by catalase and inhibited by indomethacin and aspirin. These results suggest that the production of H2O2 is involved in subsequent activation of inflammatory enzymes, such as thromboxane. Casca LAO also inhibited the bacterial growth of Gram-negative (Xanthomonas axonopodis pv passiflorae) and Gram-positive (S. mutans) strains. Electron microscopy assessments of both bacterial strains suggest that the hydrogen peroxide produced by LAO induce bacterial membrane rupture and consequently loss of cytoplasmatic content. This LAO exhibited a high antileishmanic activity against the promastigote of Leishmania amazonensis in vitro, its activity was dependent on the production of hydrogen peroxide, and the 50% inhibitory concentration was estimated in 2.39 μg/ml. © 2005 Elsevier Ltd. All rights reserved.
dc.description.firstpage47
dc.description.issuenumber1
dc.description.lastpage57
dc.description.volume47
dc.identifier.doi10.1016/j.toxicon.2005.09.008
dc.identifier.issn0041-0101
dc.identifier.urihttps://dspace.mackenzie.br/handle/10899/37836
dc.relation.ispartofToxicon
dc.rightsAcesso Restrito
dc.subject.otherlanguageAntibacterial
dc.subject.otherlanguageAntimicrobial
dc.subject.otherlanguageCrotalus durissus cascavella
dc.subject.otherlanguageGyroxin
dc.subject.otherlanguageHydrogen peroxide
dc.subject.otherlanguageLeishmanicidal
dc.titleIsolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom
dc.typeArtigo
local.scopus.citations101
local.scopus.eid2-s2.0-29944432963
local.scopus.updated2024-05-01
local.scopus.urlhttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=29944432963&origin=inward
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