CHARACTERIZATION OF A NEW LEIUROTOXIN-I-LIKE SCORPION TOXIN - PO5 FROM ANDROCTONUS-MAURETANICUS MAURETANICUS

被引：69

作者：

ZERROUK, H

MANSUELLE, P

BENSLIMANE, A

ROCHAT, H

MARTINEAUCLAIRE, MF

机构：

[1] FAC MED NORD,BIOCHIM LAB,CNRS,URA 1455,BD PIERRE DRAMARD,F-13326 MARSEILLE 15,FRANCE

[2] INST PASTEUR MAROC,PURIFICAT PROT LAB,CASABLANCA,MOROCCO

来源：

FEBS LETTERS | 1993年 / 320卷 / 03期

关键词：

SCORPION TOXIN; STRUCTURE; POTASSIUM CHANNEL; APAMIN;

D O I：

10.1016/0014-5793(93)80583-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 [I-125]apamin to rat brain synaptosomes. PO1, PO2 and PO5 have K0.5 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.

引用

页码：189 / 192

页数：4

共 23 条

[1] SCYLLATOXIN, A BLOCKER OF CA2+-ACTIVATED K+ CHANNELS - STRUCTURE-FUNCTION-RELATIONSHIPS AND BRAIN LOCALIZATION OF THE BINDING-SITES [J].