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

dc.creatorCorasolla Carregari, Victor
dc.creatorStuani Floriano, Rafael
dc.creatorRodrigues-Simioni, Lea
dc.creatorWinck, Flavia V
dc.creatorBaldasso, Paulo Aparecido
dc.creatorPonce-Soto, Luis Alberto
dc.creatorMarangoni, Sergio
dc.date2013
dc.date2015-11-27T13:31:30Z
dc.date2015-11-27T13:31:30Z
dc.date.accessioned2018-03-29T01:17:24Z
dc.date.available2018-03-29T01:17:24Z
dc.identifierBiomed Research International. v. 2013, p. 612649, 2013.
dc.identifier2314-6141
dc.identifier10.1155/2013/612649
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/23509754
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/200534
dc.identifier23509754
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1300767
dc.descriptionBbil-TX, a PLA2, was purified from Bothriopsis bilineata snake venom after only one chromatographic step using RP-HPLC on μ-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. PLA2 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 Cd(2+), Zn(2+), Mn(2+), and Mg(2+) it was reduced in the presence or absence of Ca(2+). 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.
dc.description2013
dc.description612649
dc.languageeng
dc.relationBiomed Research International
dc.relationBiomed Res Int
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBothrops
dc.subjectCalcium
dc.subjectCell Line
dc.subjectEdema
dc.subjectHydrogen-ion Concentration
dc.subjectHydrolysis
dc.subjectInflammation
dc.subjectInterleukin-1
dc.subjectInterleukin-6
dc.subjectMass Spectrometry
dc.subjectMice
dc.subjectMice, Inbred Balb C
dc.subjectMolecular Sequence Data
dc.subjectPhospholipases A2
dc.subjectPhospholipases A2, Secretory
dc.subjectReptilian Proteins
dc.subjectSnake Venoms
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.subjectTumor Necrosis Factor-alpha
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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