Characterization of a new leiurotoxin I‐like scorpion toxin

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Abstract
Three novel peptide inhibitors of the SK Ca channels were purified to homogeneity from the venom of the scorpion Androctonus mauretanicus mauretanicus using one step of RP-HPLC and competition assays with [ 125 I]apamin to rat brain synaptosomes. PO i , PO 2 and PO 5 have K 0.5 of 100,100 and 0.02 nM, respectively, for the apamin binding site. The sequence of PO 5 was established and compared to that of other scorpion toxins active on K + channels: it contains 31 residues and has a free carboxyl end. It shares sequence similarity with apamin and leiurotoxin I.