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Mono[3H]propionyl-alpha-bungarotoxin, prepared with N-succinimidyl [2,3-3H]propionate (sp. radioactivity 50 Ci/mmol) and purified to homogeneity by electrofocusing, retains its biological activity and stability. Rate constants for its binding to acetylcholine receptor were 4.4-fold lower than for unlabelled toxin; no dissociation was detectable. Analysis of enzymic digests of toxin showed 3H is located mainly of entirely in epsilon-propionyl-lysine.
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