Biochemical, pharmacological and structural characterization of a new PLA(2) from Crotalus durissus terrificus (South american rattlesnake) venom

dc.creatorHernandez-Oliveira, S
dc.creatorToyama, MH
dc.creatorToyama, DO
dc.creatorMarangoni, S
dc.creatorHyslop, S
dc.creatorRodrigues-Simioni, L
dc.date2005
dc.dateMAY
dc.date2014-11-15T04:24:44Z
dc.date2015-11-26T16:30:47Z
dc.date2014-11-15T04:24:44Z
dc.date2015-11-26T16:30:47Z
dc.date.accessioned2018-03-28T23:11:50Z
dc.date.available2018-03-28T23:11:50Z
dc.identifierProtein Journal. Springer, v. 24, n. 4, n. 233, n. 242, 2005.
dc.identifier1572-3887
dc.identifierWOS:000233246300005
dc.identifier10.1007/s10930-005-6718-z
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/55531
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/55531
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/55531
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270048
dc.descriptionA new PLA(2) (F16) was purified from Crotalus durissus terrificus venom by molecular exclusion chromatography followed by analytical reverse phase HPLC. The PLA(2) (14.86 kDa by MALDI-TOF mass spectrometry) had an amino acid sequence of SLLQFNKMIKFETRKNAVPFYAFYGCYCGWGGRRRPKDATDRCCFVHDCCYEKVTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNGYMFYPDSRCRGPSETC, and showed highly conserved Ca2+-binding and catalytic sites. F16 showed allosteric behavior with 10 mM Ca2+ and had temperature and pH optima of 25 degrees C and 7.9, respectively. F16 (10 mu g/ml) produced neuromuscular blockade in chick biventer cervicis preparations in the absence and presence of crotapotin, indicating that crotapotin was not essential for neuromuscular action in this preparation. In contrast, in mouse phrenic nerve-diaphragm preparations, the neuromuscular blockade produced by the same concentration of toxin was dependent on crotapotin. Pre-incubation with heparin markedly reduced the neurotoxicity of F16. These results show that the biochemical and structural properties of F16 are similar to those of the PLA(2) isoforms F15 and F17, but that the neurotoxicity and the requirement for crotapotin to form the crotoxin complex varies according to the neuromuscular preparation.
dc.description24
dc.description4
dc.description233
dc.description242
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationProtein Journal
dc.relationProtein J.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectCrotalus durissus terrificus
dc.subjectcrotapotin
dc.subjectcrotoxin
dc.subjectneuromuscular blockade
dc.subjectphospholipase A(2)
dc.subjectrattlesnake venom
dc.subjectPhospholipase A(2) Enzymes
dc.subjectAmino-acid-sequence
dc.subjectSnake-venom
dc.subjectEnzymatic Characterization
dc.subjectBiological-activities
dc.subjectCrotoxin Isoforms
dc.subjectCascavella
dc.subjectCollilineatus
dc.subjectNeurotoxin
dc.subjectInsights
dc.titleBiochemical, pharmacological and structural characterization of a new PLA(2) from Crotalus durissus terrificus (South american rattlesnake) venom
dc.typeArtículos de revistas


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