DETECTION OF MARINE TOXINS USING RECONSTITUTED SODIUM-CHANNELS

Specific binding of the marine toxins saxitoxin, tetrodotoxin, and bre vetoxin to the rat brain sodium channel is demonstrated using purified sodium channels reconstituted into phospholipid vesicles. Restoration of sodium channel function and binding activity by incorporation into phospholipid vesicles provides the only rigorous proof that the purif ied protein contains the neurotoxin receptor sites. In addition, recon stitution provides a valuable experimental preparation for biochemical analysis of neurotoxin binding sites and may facilitate the developme nt of a specific toxin detection system.