Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194341
Type: Artigo de periódico
Title: Tstx-iv, A Short Chain Four-disulfide-bridged Neurotoxin From Tityus Serrulatus Venom Which Acts On Ca2+-activated K+ Channels.
Author: Novello, J C
Arantes, E C
Varanda, W A
Oliveira, B
Giglio, J R
Marangoni, S
Abstract: The 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.
Subject: Amino Acid Sequence
Animals
Calcium
Disulfides
Drug Interactions
Endopeptidases
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Patch-clamp Techniques
Potassium Channels
Scorpion Venoms
Trypsin
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10082164
Date Issue: 1999
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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