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

Autor:	F. J. Joubert
Jazyk:	afrikánština
Rok vydání:	1984
Předmět:	chemistry.chemical_classification Toxin Protein primary structure Venom Biology medicine.disease_cause biology.organism_classification Amino acid Black mamba Biochemistry chemistry lcsh:Technology (General) medicine Neurotoxin lcsh:T1-995 lcsh:Q lcsh:Science Peptide sequence Cysteine
Zdroj:	South African Journal of Science and Technology, Vol 3, Iss 3, Pp 169-174 (1984)
ISSN:	2222-4173 0254-3486
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f36e5648fb8018fde83abe658352b358 http://www.satnt.ac.za/index.php/satnt/article/view/1084 Zobrazit plný text záznamu