Characterization of a new leiurotoxin I‐like scorpion toxin

FEBS Letters

Benslimane, A.²  Rochat, H.¹  Mansuelle, P.¹  Zerrouk, H.²  Martin-Eauclaire, M.F.¹ 

[1] Ingénierie des Protéines CNRS, URA 1455, Laboratoire de Biochimie, Faculté de Médecine Nord, Bd. Pierre-Dramard, 13916 Marseille Cédex 20, France;Institut Pasteur du Maroc, Laboratoire de Purification des Protéines, 1, Place Charles-Nicole, BP 120 Casablanca, Morocco

关键词: Scorpion toxin;    Structure;    Potassium channel;    Apamin;   

DOI  :  10.1016/0014-5793(93)80583-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 [¹²⁵I]apamin to rat brain synaptosomes. PO_i, PO₂ and PO₅ have K _0.5 of 100,100 and 0.02 nM, respectively, for the apamin binding site. The sequence of PO₅ 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.

【 授权许可】

Unknown