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• W2014555962 endingPage "21316" @default.
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• W2014555962 abstract "Abstract The spider toxin ω-agatoxin IIIA (ω-Aga-IIIA) is a potent inhibitor of high voltage-activated calcium currents in the mammalian brain. To establish the biochemical parameters governing its action, we radiolabeled the toxin and examined its binding to native and recombinant calcium channels. In experiments with purified rat synaptosomal membranes, both kinetic and equilibrium data demonstrate one-to-one binding of ω-Aga-IIIA to a single population of high affinity sites, with K d = ∼9 pm andB max = ∼1.4 pmol/mg protein. Partial inhibition of ω-Aga-IIIA binding by ω-conotoxins GVIA, MVIIA, and MVIIC identifies N and P/Q channels as components of this population. ω-Aga-IIIA binds to recombinant α1B and α1E calcium channels with a similar high affinity (K d = ∼5–9 pm) in apparent one-to-one fashion. Results from recombinant α1B binding experiments demonstrate virtually identicalB max values for ω-Aga-IIIA and ω-conotoxin MVIIA, providing further evidence for a one-to-one stoichiometry of agatoxin binding to calcium channels. The combined evidence suggests that ω-Aga-IIIA defines a unique, high affinity binding site on N-, P/Q-, and R-type calcium channels." @default.
• W2014555962 created "2016-06-24" @default.
• W2014555962 creator A5056599164 @default.
• W2014555962 creator A5088251178 @default.
• W2014555962 date "2000-07-01" @default.
• W2014555962 modified "2023-09-26" @default.
• W2014555962 title "The Spider Toxin ω-Aga IIIA Defines a High Affinity Site on Neuronal High Voltage-activated Calcium Channels" @default.
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• W2014555962 doi "https://doi.org/10.1074/jbc.m000212200" @default.
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