Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom

Wilkinson, MC, Nightingale, DJH, Harrison, Robert and Wagstaff, Simon ORCID: https://orcid.org/0000-0003-0577-5537 (2017) 'Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom'. Toxicon, Vol 137, pp. 92-94.

Text Wagstaff-Toxicon-2017.pdf - Accepted Version Available under License Creative Commons Attribution Non-commercial No Derivatives. Download (823kB)

Abstract

Three aspartic proteases (SVAPs) have been isolated from venom of the saw-scaled viper, Echis ocellatus. In confirmation of prior transcriptomic predictions, all three forms match to sequences of either of the two SVAP transcripts (EOC00051 and EOC00123), have a molecular weight of 42 kDa and possess a single N-glycan. The SVAPs act in a renin-like manner, specifically cleaving human and porcine angiotensinogen into angiotensin-1 and possess no general protease activity. Their activity is completely inhibited by the aspartyl protease inhibitor Pepstatin A.

Item Type:	Article
Subjects:	QS Anatomy > QS 4 General works. Classify here works on regional anatomy QU Biochemistry > Enzymes > QU 138 Ligases WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles
Faculty: Department:	Biological Sciences > Department of Tropical Disease Biology
Digital Object Identifer (DOI):	https://doi.org/10.1016/j.toxicon.2017.07.008
Depositing User:	Stacy Murtagh
Date Deposited:	01 Aug 2017 15:33
Last Modified:	17 Sep 2019 13:33
URI:	https://archive.lstmed.ac.uk/id/eprint/7416

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