Properties and biosynthesis of a neurotoxic protein of the venoms of s snakes Laticauda laticaudata and Laticauda colubrina.
1. A neurotoxic protein similar to erabutoxins a and b of Laticauda semifasciata was isolated in crystalline form from the venoms of Laticauda laticaudata and Laticauda colubrina. The name ;laticotoxin a' is proposed. 2. Laticotoxin a is homogeneous by CM-cellulose column chromatography, disc electrophoresis and ultracentrifugation and by terminal amino acid analyses. 3. Laticotoxin a consists of 62 amino acid residues. The molecular weight by ultracentrifuging is 6520. 4. The minimal 50% lethal dose of laticotoxin a by intramuscular injection to mice is 0.13mug./g. body wt. The toxin attacks the postsynaptic membrane, competing with acetylcholine. 5. Radioactive amino acids are incorporated into laticotoxin a in vivo. The incorporation is inhibited by puromycin, suggesting that the biosynthesis of the toxin follows the mechanism of protein biosynthesis, although the toxin molecule is rather small as a protein.
D000109:Acetylcholine / Q000494:pharmacology; D000818:Animals; D002845:Chromatography; D004589:Electrophoresis, Disc; D007273:Injections, Intramuscular; D008566:Membranes / Q000187:drug effects; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011691:Puromycin / Q000494:pharmacology; D012911:Snakes; D013569:Synapses; D014118:Toxins, Biological / Q000032:analysis / Q000096:biosynthesis* / Q000494:pharmacology; D014461:Ultracentrifugation; D014688:Venoms / Q000032:analysis*
D014118:Toxins, Biological; D014688:Venoms; D011691:Puromycin; D000109:Acetylcholine