Tstx-iv, A Short Chain Four-disulfide-bridged Neurotoxin From Tityus Serrulatus Venom Which Acts On Ca2+-activated K+ Channels.

dc.creatorNovello, J C
dc.creatorArantes, E C
dc.creatorVaranda, W A
dc.creatorOliveira, B
dc.creatorGiglio, J R
dc.creatorMarangoni, S
dc.date1999-Apr
dc.date2015-11-27T12:19:33Z
dc.date2015-11-27T12:19:33Z
dc.date.accessioned2018-03-29T00:53:25Z
dc.date.available2018-03-29T00:53:25Z
dc.identifierToxicon : Official Journal Of The International Society On Toxinology. v. 37, n. 4, p. 651-60, 1999-Apr.
dc.identifier0041-0101
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/10082164
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194341
dc.identifier10082164
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294574
dc.descriptionThe primary structure of TsTX-IV, a neurotoxin isolated from Tityrus serrulatus scorpion venom, is reported. Its amino acid sequence was determined by automated Edman sequential degradation of the reduced and carboxymethylated toxin and of relevant peptides obtained by digestion with Staphylococcus aureus strain V8 protease or trypsin and cleavage by CNBr. The complete sequence showed 41 amino acid residues, which account for an estimated molecular weight of 4520, and eight half-cystine residues which cross-link the toxin molecule with four disulfide bonds. The molecular weight determined by mass spectrometry was 4518. Comparison of this sequence with those from other scorpion toxins showed a resemblance with toxins which act on different types of K+ channels. TsTx-IV was able to block Ca2+-activated K+ channels of high conductance. TsTX-IV is the first four-disulfide-bridged short toxin from T. serrulatus so far completely sequenced.
dc.description37
dc.description651-60
dc.languageeng
dc.relationToxicon : Official Journal Of The International Society On Toxinology
dc.relationToxicon
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCalcium
dc.subjectDisulfides
dc.subjectDrug Interactions
dc.subjectEndopeptidases
dc.subjectMass Spectrometry
dc.subjectMolecular Sequence Data
dc.subjectMolecular Weight
dc.subjectPatch-clamp Techniques
dc.subjectPotassium Channels
dc.subjectScorpion Venoms
dc.subjectTrypsin
dc.titleTstx-iv, A Short Chain Four-disulfide-bridged Neurotoxin From Tityus Serrulatus Venom Which Acts On Ca2+-activated K+ Channels.
dc.typeArtículos de revistas


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