Isolation and characterization of renin-like aspartic-proteases from <i>Echis ocellatus</i> venom

Wilkinson, MC, Nightingale, DJH, Harrison, RA and Wagstaff, SC (2017) Isolation and characterization of renin-like aspartic-proteases from <i>Echis ocellatus</i> venom. TOXICON, 137. pp. 92-94. ISSN 0041-0101, 1879-3150

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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
Uncontrolled Keywords:	Aspartic protease, Echis ocellatus, Hypertension, Renin
Depositing User:	Symplectic Admin
Date Deposited:	28 Jul 2017 15:20
Last Modified:	06 Dec 2024 22:39
DOI:	10.1016/j.toxicon.2017.07.008
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3008680