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Journal Article

Synthesis and characterization of an N-terminal-specific 125I-photoaffinity derivative of μ-Conotoxin GIIIA which binds to the voltage-dependent sodium channel

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Becker,  Stefan
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Gordon,  Robert D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Becker, S., Liebe, R., & Gordon, R. D. (1990). Synthesis and characterization of an N-terminal-specific 125I-photoaffinity derivative of μ-Conotoxin GIIIA which binds to the voltage-dependent sodium channel. FEBS Letters, 272(1-2), 152-154. doi:10.1016/0014-5793(90)80471-T.


Cite as: https://hdl.handle.net/21.11116/0000-0007-9333-9
Abstract
An N-terminal, iodinatable photoaffinity derivative of μ-Conotoxin GIIIA, 4-Azido-salicylyl-μ-Conotoxin GIIIA (CTXASA), was synthesized by solid phase peptide synthesis. The binding of 125-CTXASA to the voltage dependent sodium channel from electroplax of Electrophorus electricus was specific, as demonstrated by saturation binding experiments. Using autoradiography, 125I-CTXASA labeled a protein with a molecular mass of 260 kDa, consistent with the apparent molecular mass of the sodium channel. This labeling could be suppressed by excess of tetrodotoxin and μ-Conotoxin GIIIA.