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Abstract
A mutant of charybdotoxin (CTX), a toxin produced from scorpion Leiurus quinquestriatus, was successfully partially purified through DEAE-cellulose chromatography.
Genes for dSlo and dSloT290E maxi-K channels were successfully transfected into HEK 293T/17 cell line that expresses no other endogenous potassium channels. During the selection period both dSlo and dSloT290E transfected cells were still able to express the maxi-K channel protein stably. This was confirmed by recording the whole cell potassium ion outward current using an electrophysiological technique: patch clamping. It also showed that the whole cell potassium outward current of HEK 293T/17 expressing dSloT290E maxi-K channels could be blocked by CTX, the dSlo maxi-K channel insensitive blocker.
