Picture of server farm and IT infrastructure

Where technology & law meet: Open Access research on data security & its regulation ...

Strathprints makes available Open Access scholarly outputs exploring both the technical aspects of computer security, but also the regulation of existing or emerging technologies. A research specialism of the Department of Computer & Information Sciences (CIS) is computer security. Researchers explore issues surrounding web intrusion detection techniques, malware characteristics, textual steganography and trusted systems. Digital forensics and cyber crime are also a focus.

Meanwhile, the School of Law and its Centre for Internet Law & Policy undertake studies on Internet governance. An important component of this work is consideration of privacy and data protection questions and the increasing focus on cybercrime and 'cyberterrorism'.

Explore the Open Access research by CIS on computer security or the School of Law's work on law, technology and regulation. Or explore all of Strathclyde's Open Access research...

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


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.