Detection of marine toxins using reconstituted sodium channels.
Specific binding of the marine toxins saxitoxin, tetrodotoxin, and brevetoxin 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 purified protein contains the neurotoxin receptor sites. In addition, reconstitution provides a valuable experimental preparation for biochemical analysis of neurotoxin binding sites and may facilitate the development of a specific toxin detection system.
Trainer
V L
VL
Department of Pharmacology, University of Washington, Seattle 98195, USA.
Baden
D G
DG
Catterall
W A
WA
D000818:Animals; D001923:Brain Chemistry; D008387:Marine Toxins / Q000302:isolation & purification* / Q000378:metabolism; D035964:Oxocins; D051381:Rats; D012530:Saxitoxin / Q000302:isolation & purification* / Q000378:metabolism; D015222:Sodium Channels / Q000378:metabolism; D013779:Tetrodotoxin / Q000302:isolation & purification* / Q000378:metabolism; D000095702:Polyether Toxins
D008387:Marine Toxins; D035964:Oxocins; D012530:Saxitoxin; D015222:Sodium Channels; D013779:Tetrodotoxin; C053342:brevetoxin; D000095702:Polyether Toxins