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Updated: Feb 26, 2026
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Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom
M C Wilkinson1, D J H Nightingale1, R A Harrison2
1Institute of Integrative Biology, University of Liverpool, Liverpool, L69 7ZB 4, UK.
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.
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