Characterization and partial purification from pheochromocytoma cells of an endogenous equivalent of scyllatoxin, a scorpion toxin which blocks small conductance Ca(2+)-activated K+ channels.
Brain Res
; 599(2): 230-6, 1992 Dec 25.
Article
in En
| MEDLINE
| ID: mdl-1337858
ABSTRACT
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 Ca(2+)-activated K+ channels (i) it competes with [125I]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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Scorpion Venoms
/
Potassium Channels
/
Calcium
Limits:
Animals
Language:
En
Journal:
Brain Res
Year:
1992
Document type:
Article
Affiliation country:
Francia