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The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

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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

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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.