Strathprints logo
Strathprints Home | Open Access | Browse | Search | User area | Copyright | Help | Library Home | SUPrimo

On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus

Chwetzoff, S. and Mollier, P. and Bouet, F. and Rowan, E.G. and Harvey, A.L. and Menez, A. (1990) On the purification of notexin: isolation of a single amino acid variant from the venom of Notechis scutatus scutatus. FEBS Letters, 261 (2). pp. 226-230. ISSN 0014-5793

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

Venom of the Australian tiger snake, Notechis scutatus scutatus was fractionated by conventional ion-exchange chromatography. The fraction containing notexin, a well-known single-chain toxic phospholipase A2, was further purified by reverse-phase high-performance liquid chromatography. Two main components were isolated and the major one corresponded to notexin. The other component, designated as notechis Ns, was an isofonn of notexin. Notechis Ns and notexin possessed similar in vitro esterase activity, in vitro neuromuscular activity and in vivo lethality. Amino acid composition and sequence of the Staphylococcus aureus V8-protease peptides demonstrated that primary structures of notechis Ns and notexin differed from each other by a single substitution amongst 119 amino acids: Lys → Arg at position 16.

Item type: Article
ID code: 17749
Keywords: notexin, isoform, phospholipase A2, reverse-phase high-performance liquid chromatography, Pharmacy and materia medica, Genetics, Biochemistry, Structural Biology, Cell Biology, Genetics, Molecular Biology, Biophysics
Subjects: Medicine > Pharmacy and materia medica
Science > Natural history > Genetics
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 11 May 2010 18:07
    Last modified: 05 Sep 2014 00:37
    URI: http://strathprints.strath.ac.uk/id/eprint/17749

    Actions (login required)

    View Item