Two new scorpion toxins that target voltage-gated Ca2+ and Na+ channels

T Olamendi-Portugal, BI García… - Biochemical and …, 2002 - Elsevier
This report describes the isolation, primary structure determination, and functional
characterization of two similar toxins from the scorpion Parabuthus granulatus named …

Synthesis and characterization of Pi4, a scorpion toxin from Pandinus imperator that acts on K+ channels

S M'Barek, A Mosbah, G Sandoz… - European journal of …, 2003 - Wiley Online Library
Pi4 is a 38‐residue toxin cross‐linked by four disulfide bridges that has been isolated from
the venom of the Chactidae scorpion Pandinus imperator. Together with maurotoxin, Pi1 …

Purification, Characterization, and Synthesis of Three Novel Toxins from the Chinese Scorpion Buthus martensi, Which Act on K+ Channels

R Romi-Lebrun, B Lebrun, MF Martin-Eauclaire… - Biochemistry, 1997 - ACS Publications
Three novel toxins belonging to the scorpion K+ channel-inhibitor family were purified to
homogeneity from the venom of the Chinese scorpion Buthus martensi. They have been …

Chemical synthesis and characterization of Pi1, a scorpion toxin from Pandinus imperator active on K+ channels

Z Fajloun, E Carlier, C Lecomte, S Geib… - European journal of …, 2000 - Wiley Online Library
Pi1 is a 35‐residue toxin cross‐linked by four disulfide bridges that has been isolated from
the venom of the chactidae scorpion Pandinus imperator. Due to its very low abundance in …

Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels

H Rochat, R Kharrat, JM Sabatier, P Mansuelle… - Toxicon, 1998 - Elsevier
Maurotoxin, a toxin from the venom of the Tunisian chactoid scorpion Scorpio maurus, has
been purified to homogeneity by gel filtration/reversed-phase HPLC, and characterized. It is …

Scorpion toxins: tools for studying K+ channels

ML Garcia, M Hanner, GJ Kaczorowski - Toxicon, 1998 - Elsevier
Over the last period of time, a large number of scorpion toxins have been characterized.
These peptidyl inhibitors of K+ channels have been very useful as probes for determining …

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

B LEBRUN, R ROMI-LEBRUN… - Biochemical …, 1997 - portlandpress.com
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 …

Structure-activity studies on scorpion toxins that block potassium channels

AL Harvey, H Vatanpour, EG Rowan, S Pinkasfeld… - Toxicon, 1995 - Elsevier
Scorpion venoms contain toxins that block different types of potassium channels. Some of
these toxins have affinity for high conductance Ca2+-activated K+ channels and for …

Scorpion toxins from Tityus cambridgei that affect Na+-channels

CVF Batista, FZ Zamudio, S Lucas, JW Fox, A Frau… - Toxicon, 2002 - Elsevier
By means of high performance liquid chromatography (HPLC) the soluble venom of the
Amazonian scorpion Tityus cambridgei was fractionated into over 50 different components …

[HTML][HTML] A new class of scorpion toxin binding sites related to an A-type K+ channel: pharmacological characterization and localization in rat brain

H Vacher, R Romi-Lebrun, C Mourre, B Lebrun… - FEBS letters, 2001 - Elsevier
A new scorpion toxin (3751.8 Da) was isolated from the Buthus martensi venom, sequenced
and chemically synthesized (sBmTX3). The A-type current of striatum neurons in culture …