dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:53:16Z
dc.date.available2014-05-20T13:53:16Z
dc.date.created2014-05-20T13:53:16Z
dc.date.issued2001-06-01
dc.identifierProtein and Peptide Letters. Hilversum: Bentham Science Publ Ltd, v. 8, n. 3, p. 179-186, 2001.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/18995
dc.identifier10.2174/0929866013409445
dc.identifierWOS:000169139300003
dc.description.abstractVenoms from Bothrops jararacussu, Bothrops asper, Bothrops atrox, Bothrops pirajai, Bothrops moojeni, Bothrops alternatus and Bothrops (Bothriopsis) bilineata were fractionated using a simplified procedure based on ion-exchange chromatography on CM-Sepharose at pH 8.0 or reverse phase HPLC. The resulting elution profiles showed important differences in the myotoxin content of these venoms. The venoms from B. alternatus, B. atrox and Bothriopsis bilineata did not contain the major myotoxin found in the other venoms. The amino acid sequence of the first 50 residues of the N-terminal region of the PLA(2)-like myotoxins showed a homology of 90-96% with other bothropic myotoxins. All of the myotoxins isolated induced rat paw edema, increased the level of plasma creatine kinase and produced myonecrosis together with polymorphonuclear cell infiltration.
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationProtein and Peptide Letters
dc.relation1.039
dc.relation0,429
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectHPLC
dc.subjectBothrops
dc.subjectphospholipase A(2)
dc.subjectand myotoxin
dc.titleComparative biochemical studies of myotoxic phospholipase A(2) from Bothrops venom
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución