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Isolation, properties and amino acid sequences of three neurotoxins from the venom of a sea snake, Aipysurus laevis
- Source :
- Biochemical Journal; January 1976, Vol. 153 Issue: 1 p79-87, 9p
- Publication Year :
- 1976
-
Abstract
- Aipysurus laevis venom was chromatographed on CM-cellulose and Bio-Rex 70 columns. Three neurotoxic components, toxins Aipysurus laevis a, b and c, were isolated. The toxins a, b and c corresponded to 22, 33 and 21% respectively of the proteins in the original venom, and accounted for almost all the lethal activity of the venom. The three toxins a, b and c were monodisperse on disc electrophoresis at pH4; toxins a and b moved at the same velocity and c a little faster. They were monodisperse also on sodium dodecyl sulphate-polyacrylamide-disc-gel electrophoresis, giving a molecular weight of 7600. The molecular weight of toxin b estimated by gel filtration was 7000. The amino acid sequence analyses of these toxins revealed that they consisted of 60 amino acid residues and that Aipysurus laevis b was [25-methionine, 28-arginine] Aipysurus laevis a. Aipysurus laevis c was [28-lysine] Aipysurus laevis a, the tryptic peptide sequence relying on homology. The LD50 values of these toxins for 20g mice were 0.076 μg/g body wt. They inhibited the acetylcholine-induced contracture but did not affect the CKl-induced contracture of the isolated muscle.
Details
- Language :
- English
- ISSN :
- 02646021 and 14708728
- Volume :
- 153
- Issue :
- 1
- Database :
- Supplemental Index
- Journal :
- Biochemical Journal
- Publication Type :
- Periodical
- Accession number :
- ejs51289706
- Full Text :
- https://doi.org/10.1042/bj1530079