Original Research

The primary structure of a short neurotoxin homologue from Dendroaspis polylepis polylepis (Black mamba) venom

F. J. Joubert
Suid-Afrikaanse Tydskrif vir Natuurwetenskap en Tegnologie | Vol 3, No 3 | a1084 | DOI: https://doi.org/10.4102/satnt.v3i3.1084 | © 1984 F. J. Joubert | This work is licensed under CC Attribution 4.0
Submitted: 20 March 1984 | Published: 20 March 1984

About the author(s)

F. J. Joubert,, South Africa

Full Text:

PDF (237KB)

Share this article

Bookmark and Share

Abstract

Toxin CM-7 was purified from black mamba venom by gel filtration on Sephadex G-50 followed by ion exchange chromotography on CM-cellulose. It contains 60 amino acids, including eight half-cystines. The complete amino acid sequence of toxin CM-7 has been elucidated. In toxin CM-7 the eleven structurally invariant amino acids of the neurotoxins and cardiotoxins are conserved, but it has only one of the five functionally invariant amino acids of the neurotoxins. The eight cysteine residues of toxin CM-7 are in the same locations as those in short neurotoxins of known structures and are presumed to be similarly cross-linked. The sequence of CM-7 is structurally homologous with the short neurotoxins, but it is less toxic.

Keywords

No related keywords in the metadata.

Metrics

Total abstract views: 953
Total article views: 957

Reader Comments

Before posting a comment, read our privacy policy.

Post a comment (login required)

Crossref Citations

No related citations found.