Tools
Tools
Hasson, S.S., Theakston, R.David G. and Harrison, Robert (2003) 'Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus'. Toxicon, Vol 42, Issue 6, pp. 629-634.
Full text not available from this repository.Abstract
Systemic envenoming by the saw-scaled viper, Echis ocellatus, is responsible for more deaths than any other snake in West Africa. Despite its medical importance, there have been few investigations into the toxin composition of the venom of this viper. Here we describe the isolation of E. ocellatus venom gland cDNAs encoding a protein of 514 amino acids that showed 91% sequence similarity to Ecarin, a prothrombin-activating metalloproteinase from the venom of the East African viper, E. pyramidum leakeyi, that induces severe consumption coagulopathy. Structural similarities between the E. ocellatus metalloproteinase and analogues in venoms of related vipers suggest that antibodies raised to phylogenetically conserved E. ocellatus metalloproteinase domains may have potential for cross-specific and cross-generic neutralisation of analogous venom toxins. (C) 2003 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Echis ocellatus; cDNA cloning; Prothrombin activator |
| Subjects: | QU Biochemistry > Genetics > QU 450 General Works 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/j.toxicon.2003.08.009 |
| Depositing User: | Ms Julia Martin |
| Date Deposited: | 30 Jun 2012 18:07 |
| Last Modified: | 06 Feb 2018 13:04 |
| URI: | https://archive.lstmed.ac.uk/id/eprint/2566 |
Statistics
Actions (login required)
 |
Edit Item |