Synthesis and characterization of an N-terminal-specific125I-photoaffinity derivative of μ-Conotoxin GIIIA which binds to the voltage-dependent sodium channel
- 15 October 1990
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 272 (1-2) , 152-154
- https://doi.org/10.1016/0014-5793(90)80471-t
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 125I-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 GIIIAKeywords
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