CHARACTERIZATION AND PARTIAL-PURIFICATION FROM PHEOCHROMOCYTOMA CELLS OF AN ENDOGENOUS EQUIVALENT OF SCYLLATOXIN, A SCORPION TOXIN WHICH BLOCKS SMALL CONDUCTANCE CA2+-ACTIVATED K+ CHANNELS

被引：9

作者：

AUGUSTE, P ^{[1
]}

HUGUES, M ^{[1
]}

BORSOTTO, M ^{[1
]}

THIBAULT, J ^{[1
]}

ROMEY, G ^{[1
]}

COPPOLA, T ^{[1
]}

LAZDUNSKI, M ^{[1
]}

机构：

[1] INST PHARMACOL MOLEC & CELLULAIRE,660 ROUTE LUCIOLES,F-06560 VALBONNE,FRANCE

来源：

BRAIN RESEARCH | 1992年 / 599卷 / 02期

关键词：

IONIC CHANNEL; ENDOGENOUS LIGAND; PHEOCHROMOCYTOMA; PURIFICATION; PEPTIDE; TOXIN; VENOM;

D O I：

10.1016/0006-8993(92)90396-Q

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

This work describes the partial purification of a heat-stable peptide which has the same properties as the scorpion toxin, scyllatoxin, a specific blocker of one class of Ca2+-activated K+ channels: (i) it competes with [I-125]apamin for binding to the same site, (ii) like apamin and scyllatoxin, it blocks the after-potential hyperpolarization in skeletal muscle cells in culture, (iii) like apamin and scyllatoxin, it contracts guinea-pig taenia coli relaxed by epinephrine, (iv) it cross-reacts with antibodies raised against scyllatoxin but not with antibodies raised against apamin.

引用

页码：230 / 236

页数：7

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