dc.contributorUniv Hamburg
dc.contributorUFZ Helmholtz Ctr Environm Res
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorBulgarian Acad Sci
dc.date.accessioned2014-05-20T14:02:34Z
dc.date.accessioned2022-10-05T14:50:51Z
dc.date.available2014-05-20T14:02:34Z
dc.date.available2022-10-05T14:50:51Z
dc.date.created2014-05-20T14:02:34Z
dc.date.issued2010-05-01
dc.identifierJournal of Proteome Research. Washington: Amer Chemical Soc, v. 9, n. 5, p. 2302-2316, 2010.
dc.identifier1535-3893
dc.identifierhttp://hdl.handle.net/11449/22055
dc.identifier10.1021/pr901042p
dc.identifierWOS:000277353200022
dc.identifier9162508978945887
dc.identifier0000-0003-2460-1145
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3895737
dc.description.abstractThe snake venomic of Crotalus durissus terrificus was analyzed by 2-D and 1-D electrophoresis and subsequent MS/MS and enzymatic assays. The venomic of the South American rattlesnake comprises toxins from seven protein families: phospholipases A(2), serine proteinases, ecto-5'-nucleotidases, metalloproteinases, nerve growth factors, phosphodiesterases, and glutaminyl cyclase. The venom toxin composition correlates with the clinical manifestation of the crotalinae snake bites and explains pathological effects of the venom such as neurotoxicity, systemic myonecrosis, hemostatic disorders, myoglobinuria, and acute renal failure. The vast majority of toxins are potentially involved in neurotoxicity, myotoxicity, and coagulopathy. The predominant venom components are neurotoxic phospholipases A2 and serine proteinases. The venom is a rich source of 5'-nucleotidases (7.8% of the identified toxins) inducing hemostatic disorders. Analysis of the venom protein composition provided a catalogue for secreted toxins. The venomic composition of Crotalus d. terrificus and venom gland transcriptome of the synonymous subspecies Crotalus d. collilineatus show differences in the occurrence of protein families and in the abundance of toxins. Some of the venom components identified by the proteomic analysis were not reported in the transcriptome of the Crotalus d. collilineatus venom gland. Enzymatic activities of the Crotalus d. terrificus venom were determined and correlated with the proteomic composition.
dc.languageeng
dc.publisherAmer Chemical Soc
dc.relationJournal of Proteome Research
dc.relation3.950
dc.relation1,818
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSnake venomic
dc.subjectCrotalus durissus terrificus
dc.subject2-D electrophoresis
dc.subjectelectrospray mass spectrometry
dc.titleSnake Venomic of Crotalus durissus terrificus-Correlation with Pharmacological Activities
dc.typeArtigo


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