Abstract
Tetrodotoxin-binding sites were covalently labelled with a highly tritiated derivative of tetrodotoxin. Cross-linking experiments, using dissucinimidyl suberate, on partially purified tetrodotoxin-binding component from electroplax of Electrophorus , electricus , revealed covalent labelling of a single polypeptide chain of MW 270,000.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have