CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom

Montamas Suntravat, Paul R. Langlais, Elda E. Sánchez, Vance G. Nielsen

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.

Original languageEnglish (US)
Pages (from-to)585-593
Number of pages9
JournalBiometals
Volume31
Issue number4
DOIs
StatePublished - Aug 1 2018

Keywords

  • Carbon monoxide
  • Heme
  • Mass spectrometry
  • Snake venom metalloproteinase
  • Thrombelastography

ASJC Scopus subject areas

  • Biomaterials
  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • Metals and Alloys

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