Biochemical, Pharmacological, And Structural Characterization Of New Basic Pla2 Bbil-tx From Bothriopsis Bilineata Snake Venom

dc.creatorCorasolla Carregari V.
dc.creatorStuani Floriano R.
dc.creatorRodrigues-Simioni L.
dc.creatorWinck F.V.
dc.creatorBaldasso P.A.
dc.creatorPonce-Soto L.A.
dc.creatorMarangoni S.
dc.date2013
dc.date2015-06-25T19:11:13Z
dc.date2015-11-26T15:08:52Z
dc.date2015-06-25T19:11:13Z
dc.date2015-11-26T15:08:52Z
dc.date.accessioned2018-03-28T22:19:08Z
dc.date.available2018-03-28T22:19:08Z
dc.identifier
dc.identifierBiomed Research International. , v. 2013, n. , p. - , 2013.
dc.identifier23146133
dc.identifier10.1155/2013/612649
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84874594438&partnerID=40&md5=44c00990723e119db6a58be2d562435b
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/88623
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/88623
dc.identifier2-s2.0-84874594438
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1257728
dc.descriptionBbil-TX, a PLA2, was purified from Bothriopsis bilineata snake venom after only one chromatographic step using RP-HPLC on μ7u-Bondapak C-18 column. A molecular mass of 14243.8 Da was confirmed by Q-Tof Ultima API ESI/MS (TOF MS mode) mass spectrometry. The partial protein sequence obtained was then submitted to BLASTp, with the search restricted to PLA2 from snakes and shows high identity values when compared to other PLA2s. PLA 2 activity was presented in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 25-37°C. Maximum PLA2 activity required Ca 2+ and in the presence of Cd2+, Zn2+, Mn 2+, and Mg2+ it was reduced in the presence or absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom and antihemorrhagic factor DA2-II from Didelphis albiventris opossum sera under optimal conditions significantly inhibit the enzymatic activity. Bbil-TX induces myonecrosis in mice. The fraction does not show a significant cytotoxic activity in myotubes and myoblasts (C2C12). The inflammatory events induced in the serum of mice by Bbil-TX isolated from Bothriopsis bilineata snake venom were investigated. An increase in vascular permeability and in the levels of TNF-a, IL-6, and IL-1 was was induced. Since Bbil-TX exerts a stronger proinflammatory effect, the phospholipid hydrolysis may be relevant for these phenomena. © 2013 Victor Corasolla Carregari et al.
dc.description2013
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dc.description
dc.description
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dc.languageen
dc.publisher
dc.relationBioMed Research International
dc.rightsaberto
dc.sourceScopus
dc.titleBiochemical, Pharmacological, And Structural Characterization Of New Basic Pla2 Bbil-tx From Bothriopsis Bilineata Snake Venom
dc.typeArtículos de revistas


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