1. Amino acid sequence of .kappa.-flavitoxin: establishment of a new family of snake venom neurotoxins
- Author
-
Gregory A. Grant, Mark W. Frazier, and Vincent A. Chiappinelli
- Subjects
Molecular Sequence Data ,Neurotoxins ,Venom ,Biology ,Biochemistry ,Bungarus ,chemistry.chemical_compound ,Species Specificity ,medicine ,Animals ,Trypsin ,Amino Acid Sequence ,Peptide sequence ,Chromatography, High Pressure Liquid ,Elapid Venoms ,Chymotrypsin ,Methionine ,Protein primary structure ,Snakes ,Anatomy ,biology.organism_classification ,Peptide Fragments ,nervous system ,chemistry ,Snake venom ,biology.protein ,medicine.drug - Abstract
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.
- Published
- 1988