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

Toxicon. 2017 Oct:137:92-94. doi: 10.1016/j.toxicon.2017.07.008. Epub 2017 Jul 19.

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.

Keywords: Aspartic protease; Echis ocellatus; Hypertension; Renin.

MeSH terms

  • Amino Acid Sequence
  • Angiotensin I / chemistry*
  • Angiotensinogen / chemistry*
  • Animals
  • Aspartic Acid Proteases / chemistry
  • Aspartic Acid Proteases / isolation & purification*
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification
  • Pepstatins / chemistry
  • Protease Inhibitors / chemistry
  • Swine
  • Viper Venoms / chemistry*
  • Viperidae*

Substances

  • Isoenzymes
  • Pepstatins
  • Protease Inhibitors
  • Viper Venoms
  • Angiotensinogen
  • Angiotensin I
  • Aspartic Acid Proteases
  • pepstatin