Amino acid sequence of kappa-flavitoxin: establishment of a new family of snake venom neurotoxins.
The complete amino acid sequence of kappa-flavitoxin, a neurotoxin isolated from the venom of Bungarus flaviceps, has been determined by automated Edman analysis of the intact protein and of peptides derived from digests with trypsin and chymotrypsin. kappa-Flavitoxin consists of a single 66-residue polypeptide chain which is completely devoid of methionine. The amino acid sequence of kappa-flavitoxin demonstrates that although the toxin is related to the alpha-neurotoxin family, it displays a much higher degree of homology with kappa-bungarotoxin. The conserved structural features of the kappa-neurotoxins and their pharmacological profiles, which are distinct from those of all known alpha-neurotoxins, provide evidence for a new, structurally and functionally unique family of snake venom neurotoxins.
Grant
G A
GA
Department of Biological Chemistry, Washington University School of Medicine, St. Louis, Missouri 63110.
Frazier
M W
MW
Chiappinelli
V A
VA
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004546:Elapid Venoms; D008969:Molecular Sequence Data; D009498:Neurotoxins; D010446:Peptide Fragments / Q000032:analysis; D012911:Snakes; D013045:Species Specificity; D014357:Trypsin
D004546:Elapid Venoms; D009498:Neurotoxins; D010446:Peptide Fragments; C052119:kappa-flavitoxin; D014357:Trypsin