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Howes, J.M., Wilkinson, M. C., Theakston, R.David G. and Laing, Gavin (2003) 'The purification and partial characterisation of two novel metalloproteinases from the venom of the West African carpet viper, Echis ocellatus'. Toxicon, Vol 42, Issue 1, pp. 21-27.
Full text not available from this repository.Abstract
Separation of previously uncharacterised Echis ocellatus venom by phenyl-Superose FPLC (Fast Liquid Protein Chromatography) yielded eight protein fractions. Three of these displayed high proteolytic activity when assayed by in vivo and in vitro assays (including enzyme linked immunosorbant assay), and were further separated using Superdex 75 and Mono-Q FPLC. This resulted in the purification of a non-haemorrhagic 24 kDa metal loproteinase (EoVMP1, p17.0), and a haemorrhagic 56 kDa metalloproteinase (EoVMP2, p15.5). Following tryptic digest, short amino acid sequences of EoVMP1 and EoVMP2 were obtained using Edman degradation. Both sequences displayed homology when aligned with existing snake venom metalloproteinases (SVMPs). The strong homology observed among previously well-characterised SVMPs suggests that principles governing the interaction of substrates and inhibitors are likely to be similar for EoVMP1, EoVMP2 and all members of the reprolysin family. (C) 2003 Elsevier Science Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Subjects: | QV Pharmacology > Toxicology > General Toxicology > QV 601 Antidotes and other therapeutic measures WA Public Health > Health Problems of Special Population Groups > WA 395 Health in developing countries WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles |
| Faculty: Department: | Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group |
| Digital Object Identifer (DOI): | https://doi.org/10.1016/s0041-0101(03)00096-5 |
| Depositing User: | Users 494 not found. |
| Date Deposited: | 22 Jan 2013 16:44 |
| Last Modified: | 06 Feb 2018 13:04 |
| URI: | https://archive.lstmed.ac.uk/id/eprint/2576 |
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