dc.creatorFagundes, F H R
dc.creatorOliveira, M
dc.creatorHuancahuire-Vega, S
dc.creatorRomero-Vargas, F F
dc.creatorPonce-Soto, L A
dc.creatorMarangoni, S
dc.date2010-Mar
dc.date2015-11-27T13:17:47Z
dc.date2015-11-27T13:17:47Z
dc.date.accessioned2018-03-29T01:10:46Z
dc.date.available2018-03-29T01:10:46Z
dc.identifierBrazilian Journal Of Medical And Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas / Sociedade Brasileira De Biofísica ... [et Al.]. v. 43, n. 3, p. 262-70, 2010-Mar.
dc.identifier1414-431X
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/20401434
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/198820
dc.identifier20401434
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1299053
dc.descriptionTo illustrate the construction of precursor complementary DNAs, we isolated mRNAs from whole venom samples. After reverse transcription polymerase chain reaction (RT-PCR), we amplified the cDNA coding for a neurotoxic protein, phospholipase A2 D49 (PLA2 D49), from the venom of Crotalus durissus collilineatus (Cdc PLA2). The cDNA encoding Cdc PLA2 from whole venom was sequenced. The deduced amino acid sequence of this cDNA has high overall sequence identity with the group II PLA2 protein family. Cdc PLA2 has 14 cysteine residues capable of forming seven disulfide bonds that characterize this group of PLA2 enzymes. Cdc PLA2 was isolated using conventional Sephadex G75 column chromatography and reverse-phase high performance liquid chromatography (RP-HPLC). The molecular mass was estimated using matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. We tested the neuromuscular blocking activities on chick biventer cervicis neuromuscular tissue. Phylogenetic analysis of Cdc PLA2 showed the existence of two lines of N6-PLA2, denominated F24 and S24. Apparently, the sequences of the New World's N6-F24-PLA2 are similar to those of the agkistrodotoxin from the Asian genus Gloydius. The sequences of N6-S24-PLA2 are similar to the sequence of trimucrotoxin from the genus Protobothrops, found in the Old World.
dc.description43
dc.description262-70
dc.languageeng
dc.relationBrazilian Journal Of Medical And Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas / Sociedade Brasileira De Biofísica ... [et Al.]
dc.relationBraz. J. Med. Biol. Res.
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectChickens
dc.subjectChromatography, High Pressure Liquid
dc.subjectChromatography, Reverse-phase
dc.subjectCrotalid Venoms
dc.subjectDna, Complementary
dc.subjectMale
dc.subjectMass Spectrometry
dc.subjectMolecular Sequence Data
dc.subjectNeuromuscular Junction
dc.subjectNeurotoxins
dc.subjectPhospholipases A2
dc.subjectPhylogeny
dc.subjectRna, Messenger
dc.subjectReverse Transcriptase Polymerase Chain Reaction
dc.titleCdna And Deduced Primary Structure Of Basic Phospholipase A2 With Neurotoxic Activity From The Venom Secretion Of The Crotalus Durissus Collilineatus Rattlesnake.
dc.typeArtículos de revistas


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