Purification and partial characterization of two phospholipases A(2) from Bothrops leucurus (white-tailed-jararaca) snake venom

dc.contributorUniv Mogi Das Cruzes
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.contributorUniversidade Federal de Minas Gerais (UFMG)
dc.creatorHiguchi, Debora Ayame
dc.creatorBarbosa, Christiano Marcello Vaz
dc.creatorBincoletto, Claudia
dc.creatorChagas, Jair Ribeiro
dc.creatorMagalhaes, Arinos
dc.creatorRichardson, Michael
dc.creatorSanchez, Eladio Flores
dc.creatorPesquero, João Bosco [UNIFESP]
dc.creatorAraújo, Ronaldo de Carvalho
dc.creatorPesquero, Jorge Luiz
dc.date.accessioned2016-01-24T12:41:55Z
dc.date.accessioned2023-09-04T18:48:54Z
dc.date.available2016-01-24T12:41:55Z
dc.date.available2023-09-04T18:48:54Z
dc.date.created2016-01-24T12:41:55Z
dc.date.issued2007-03-01
dc.identifierBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 89, n. 3, p. 319-328, 2007.
dc.identifier0300-9084
dc.identifierhttps://repositorio.unifesp.br/handle/11600/29540
dc.identifier10.1016/j.biochi.2006.10.010
dc.identifierWOS:000245998900006
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8619358
dc.description.abstractTwo proteins with phospholipase A(2) (PLA(2)) activity were purified to homogeneity from Bothrops leucurus (white-tailed-jararaca) snake venom through three chromatographic steps: Conventional gel filtration on Sephacryl S-200, ion-exchange on Q-Sepharose and reverse phase on Vydac C4 HPLC column. the molecular mass for both enzymes was estimated to be approximately 14 kDa by SDS-PAGE. the N-terminal sequences (48 residues) show that one enzyme presents lysine at position 48 and the other an aspartic acid in this position, and therefore they were designated blK-PLA(2) and blD-PLA(2) respectively. blK-PLA(2) presented negligible levels of PLA(2) activity as compared to that of blD-PLA(2). the PLA(2) activity of both enzymes is Ca2+-dependent. blD-PLA(2) did not have any effect upon platelet aggregation induced by arachidonic acid, ADP or collagen, but strongly inhibits coagulation and is able to stimulate Ehrlich tumor growth but not angiogenesis. (c) 2006 Elsevier Masson SAS. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimie
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.rightsAcesso restrito
dc.subjectBothrops leucurus
dc.subjectPLA(2)
dc.subjectPlatelet aggregation
dc.subjectBlood coagulation
dc.subjectAngiogenesis
dc.subjectSnake venom
dc.titlePurification and partial characterization of two phospholipases A(2) from Bothrops leucurus (white-tailed-jararaca) snake venom
dc.typeArtigo


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