A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom

A new toxin, named HsTX1, has been identified in the venom of Heterometrus spinnifer (Scorpionidae), on the basis of its ability to block the rat Kv1.3 channels expressed in Xenopus oocytes. HsTX1 has been purified and characterized as a 34-residue peptide reticulated by four disulphide bridges. HsT...

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Veröffentlicht in:	Biochemical journal 1997-11, Vol.328 ( Pt 1) (1), p.321-327
Hauptverfasser:	Lebrun, B, Romi-Lebrun, R, Martin-Eauclaire, M F, Yasuda, A, Ishiguro, M, Oyama, Y, Pongs, O, Nakajima, T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides - metabolism Amino Acid Sequence Animals Binding, Competitive Biological Assay Disulfides - chemistry Genetic Vectors Ion Channel Gating Kv1.3 Potassium Channel Molecular Sequence Data Molecular Weight Oocytes Potassium Channel Blockers Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated Rats Scorpion Venoms - biosynthesis Scorpion Venoms - chemistry Scorpion Venoms - isolation & purification Scorpion Venoms - metabolism Sequence Analysis Sequence Homology, Amino Acid Xenopus
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