Next Article in Journal
Protein-Bound Uremic Toxins: New Insight from Clinical Studies
Previous Article in Journal
Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX)
Article Menu

Export Article

Open AccessArticle
Toxins 2011, 3(7), 900-910; doi:10.3390/toxins3070900

Isolation and Biochemical Characterization of Rubelase, a Non-Hemorrhagic Elastase from Crotalus ruber ruber (Red Rattlesnake) Venom

1
Department of Microbiology, Faculty of Pharmacy, Meijo University, 150 Yagotoyama, Tenpaku, Nagoya 468-8503, Japan
2
Suntory Institute for Bioorganic Research, Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan
*
Author to whom correspondence should be addressed.
Received: 9 May 2011 / Revised: 28 June 2011 / Accepted: 12 July 2011 / Published: 19 July 2011
View Full-Text   |   Download PDF [420 KB, uploaded 19 July 2011]   |  

Abstract

A novel non-hemorrhagic basic metalloprotease, rubelase, was isolated from the venom of Crotalus ruber ruber. Rubelase hydrolyzes succinyl-L-alanyl-L-alanyl-L-alanyl p-nitroanilide (STANA), a specific substrate for elastase, and the hydrolytic activity was inhibited by chelating agents. It also hydrolyzes collagen and fibrinogen. However, hemorrhagic activity was not observed. By ESI/Q-TOF and MALDI/TOF mass spectrometry combined with Edman sequencing procedure, the molecular mass of rubelase was determined to be 23,266 Da. Although its primary structure was similar to rubelysin (HT-2), a hemorrhagic metalloprotease isolated from the same snake venom, the circumstances surrounding putative zinc binding domain HEXXHXXGXXH were found to be different when the three-dimensional computer models of both metalloproteases were compared. The cytotoxic effects of rubelase and rubelysin on cultured endothelial and smooth muscle cells were also different, indicating that the substitution of several amino acid residues causes the changes of active-site conformation and cell preference.
Keywords: Crotalus ruber ruber toxin; elastase; amino acid sequence; cytotoxicity Crotalus ruber ruber toxin; elastase; amino acid sequence; cytotoxicity
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Komori, Y.; Sakai, K.; Masuda, K.; Nikai, T. Isolation and Biochemical Characterization of Rubelase, a Non-Hemorrhagic Elastase from Crotalus ruber ruber (Red Rattlesnake) Venom. Toxins 2011, 3, 900-910.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top