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J. Biol. Chem., Vol. 263, Issue 21, 10192-10197, 07, 1988
GG Chicchi, G Gimenez-Gallego, E Ber, ML Garcia, R Winquist and MA Cascieri
An inhibitor of apamin binding has been purified to homogeneity in three
chromatographic steps from the venom of the scorpion, Leiurus
quinquestriatus hebraeus. The inhibitor, which we have named leiurotoxin I,
represents less than 0.02% of the venom protein. It is a 3.4-kDa peptide
with little structural homology to apamin although it has some homology to
other scorpion toxins such as charybdotoxin, noxiustoxin, and neurotoxin
P2. Leiurotoxin I completely inhibits 125I- apamin binding to rat brain
synaptosomal membranes (Ki = 75 pM). Thus, it is 10-20-fold less potent
than apamin. Leiurotoxin I is not a strictly competitive inhibitor of this
binding reaction. Like apamin, leiurotoxin I blocks the epinephrine-induced
relaxation of guinea pig teniae coli (ED50 = 6.5 nM), while having no
effect on the rate or force of contraction in guinea pig atria or rabbit
portal vein preparations. Thus, leiurotoxin I of scorpion venom and apamin
of honeybee venom demonstrate similar activities in a variety of tissues,
yet are structurally unrelated peptides. These two peptides should be
useful in elucidating the role of the small conductance, Ca2+-activated K+
channels in different tissues.
Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom
Merck Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065- 0900.
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