Abstract
The complete amino acid sequence of κ-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.κ-Flavitoxin consists of a single 66-residue polypeptide chain which is completely devoid of methionine. the amino acid sequence of κ-flavitoxin demonstrates that although the toxin is related to the α-neurotoxin family, it displays a much higher degree of homology with κ-bungarotoxin. the conserved structural features of the K-neurotoxins and their pharmacological profiles, which are distinct from those of all known α-neurotoxins, provide evidence for a new, structurally and functionally unique family of snake venom neurotoxins.
Original language | English |
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Pages (from-to) | 3794-3798 |
Number of pages | 5 |
Journal | Biochemistry |
Volume | 27 |
Issue number | 10 |
DOIs | |
State | Published - May 1 1988 |