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

Mark Wilkinson; D. J.H. Nightingale; Robert Harrison; Simon Wagstaff

doi:10.1016/j.toxicon.2017.07.008

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

Mark Wilkinson, D. J.H. Nightingale, Robert Harrison, Simon Wagstaff

Tropical Disease Biology

University of Liverpool

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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.

Original language	English
Pages (from-to)	92-94
Number of pages	3
Journal	Toxicon
Volume	137
Early online date	19 Jul 2017
DOIs	https://doi.org/10.1016/j.toxicon.2017.07.008
Publication status	E-pub ahead of print - 19 Jul 2017

Keywords

Aspartic protease
Echis ocellatus
Hypertension
Renin

Access to Document

10.1016/j.toxicon.2017.07.008

Wagstaff-Toxicon-2017Accepted author manuscript, 804 KBLicence: CC BY-NC-ND

Cite this

@article{8b38f70d3d8040f282a5ffac6563d8fc,

title = "Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom",

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",

author = "Mark Wilkinson and Nightingale, \{D. J.H.\} and Robert Harrison and Simon Wagstaff",

year = "2017",

month = jul,

day = "19",

doi = "10.1016/j.toxicon.2017.07.008",

language = "English",

volume = "137",

pages = "92--94",

journal = "Toxicon",

issn = "0041-0101",

publisher = "Elsevier Ltd",

}

TY - JOUR

T1 - Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom

AU - Wilkinson, Mark

AU - Nightingale, D. J.H.

AU - Harrison, Robert

AU - Wagstaff, Simon

PY - 2017/7/19

Y1 - 2017/7/19

N2 - 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.

AB - 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.

KW - Aspartic protease

KW - Echis ocellatus

KW - Hypertension

KW - Renin

U2 - 10.1016/j.toxicon.2017.07.008

DO - 10.1016/j.toxicon.2017.07.008

M3 - Article

SN - 0041-0101

VL - 137

SP - 92

EP - 94

JO - Toxicon

JF - Toxicon

ER -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this