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

Authors :: Wilkinson MC
Nightingale DJH
Harrison RA
Wagstaff SC
Source :: Toxicon : official journal of the International Society on Toxinology [Toxicon] 2017 Oct; Vol. 137, pp. 92-94. Date of Electronic Publication: 2017 Jul 19.
Publication Year :: 2017
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.<br /> (Copyright © 2017 Elsevier Ltd. All rights reserved.)

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

Language :: English
ISSN :: 1879-3150
Volume :: 137
Database :: MEDLINE
Journal :: Toxicon : official journal of the International Society on Toxinology
Publication Type :: Academic Journal
Accession number :: 28734982
Full Text :: https://doi.org/10.1016/j.toxicon.2017.07.008

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