A prothrombin activator serine protease from the Lonomia obliqua caterpillar venom (Lopap) biochemical characterization

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dc.contributor.authorReis, C. V.
dc.contributor.authorPortaro, FCV
dc.contributor.authorAndrade, S. A.
dc.contributor.authorFritzen, M.
dc.contributor.authorFernandes, B. L.
dc.contributor.authorSampaio, CAM
dc.contributor.authorCamargo, ACM
dc.contributor.authorChudzinski-Tavassi, A. M.
dc.contributor.institutionFAPESP
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T12:31:24Z
dc.date.available2016-01-24T12:31:24Z
dc.date.issued2001-06-01
dc.description.abstractLonomia obliqua venom causes a severe consumptive coagulopathy, which can lead to a hemorrhagic syndrome. the crude bristles extract displays a procoagulant activity due to a Factor X and to a prothrombin activating activity. Here, we describe a 69 kDa prothrombin activator serine protease purified from L. obliqua caterpillar bristle extract using gel filtration (Sephadex G 75) and HPLC (C-4 column). the purified protein was able to activate prothrombin in a dose-dependent manner, and calcium ions increased this activity. the prothrombin-derived fluorogenic peptide (Abz-YQTFFNPRTGSQ-EDDnp) had its main cleavage site at the Arg-Thr bond. the kinetic parameters obtained for this substrate were K-mapp. of 4.5 muM, k(cat) of 5.32 s(-1), and a k(cat)/K-mapp of 1.2 x 10(6) M-1 s(-1). the prothrombin fragments generated by the purified enzyme corresponded to the molecular masses of prethrombin 2, fragment 1, fragment 2, and thrombin as seen in SDS-PAGE. the thrombin generated was able to clot purified fibrinogen. the partial amino acid sequence of the purified protein, named Lopap (L. obliqua prothrombin activator protease), showed no similarity to any known prothrombin activator. (C) 2001 Elsevier B.V. All rights reserved.en
dc.description.affiliationFAPESP, Biochem & Biophys Lab, Butantan Inst, Ctr Appl Toxinol,CEPID, BR-05503900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem & Mol Biol, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Dept Microbiol, Inst Biomed Sci, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem & Mol Biol, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent427-436
dc.identifierhttp://dx.doi.org/10.1016/S0049-3848(01)00265-1
dc.identifier.citationThrombosis Research. Oxford: Pergamon-Elsevier B.V., v. 102, n. 5, p. 427-436, 2001.
dc.identifier.doi10.1016/S0049-3848(01)00265-1
dc.identifier.issn0049-3848
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26569
dc.identifier.wosWOS:000169278900006
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofThrombosis Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectLonomia obliquaen
dc.subjectprothrombin activatoren
dc.subjectcoagulopathyen
dc.subjectcaterpillaren
dc.titleA prothrombin activator serine protease from the Lonomia obliqua caterpillar venom (Lopap) biochemical characterizationen
dc.typeinfo:eu-repo/semantics/article
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