Literature DB >> 1164509

Snake venom toxins. The primary structure of protein S4C11. A neurotoxin homologue from the venom of forest cobra (Naja melanoleuca).

F H Carlsson.   

Abstract

Six minor protein constituents (S4C10-S4C15) have been isolated from the venom of Naja melanoleuca. The complete amino acid sequence of S4C11 has been established and indicates that it is a homologue of the neurotoxins which are found in elapid venoms. The other proteins appear from the amino acid compositions to be homologues of the cyto- or cardiotoxins found in cobra venoms. Protein S4C11 has a low toxicity, failing to kill mice at an intravenous dose of 20 mug/g body weight. The sequence of the first 25 residues out of the total of 65, was determined using the automatic sequenator. The remainder of the sequence was derived with the aid of tryptic and chymotryptic peptides. The sequence showed the unusual feature of having 65 amino acid residues including 10 half-cystine residues.

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Year:  1975        PMID: 1164509     DOI: 10.1016/0005-2795(75)90186-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

Review 1.  From toxins targeting ligand gated ion channels to therapeutic molecules.

Authors:  Adak Nasiripourdori; Valérie Taly; Thomas Grutter; Antoine Taly
Journal:  Toxins (Basel)       Date:  2011-03-21       Impact factor: 4.546

2.  A Neurotoxic Snake Venom without Phospholipase A2: Proteomics and Cross-Neutralization of the Venom from Senegalese Cobra, Naja senegalensis (Subgenus: Uraeus).

Authors:  Kin Ying Wong; Kae Yi Tan; Nget Hong Tan; Choo Hock Tan
Journal:  Toxins (Basel)       Date:  2021-01-14       Impact factor: 4.546

  2 in total

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