• Title of article

    Enzymatic Analysis of Iranian Echis carinatus Venom Using Zymography

  • Author/Authors

    Kamyab, Mostafa Faculty of Biological Sciences - Shahid Beheshti University, Tehran, Iran , Kim, Euikyung Department of Pharmacology and Toxicology - College of Veterinary Medicine - Gyeongsang National University, Jinju, South Korea , Hoseinyc, Mehdi Department of Pharmacology and Toxicology - Bushehr University of Medical Sciences, Bushehr, Iran , Seyedianc, Ramin Department of Pharmacology and Toxicology - Bushehr University of Medical Sciences, Bushehr, Iran

  • Pages
    6
  • From page
    1155
  • To page
    1160
  • Abstract
    Snakebite is a common problem especially in tropical areas all over the world including Iran. Echis carinatus as one of the most dangerous Iranian snakes is spreading in this country excluding central and northwest provinces. In this study gelatinase and fibrinogenolytic properties as two disintegrating matrix metalloproteinase enzymes were evaluated by a strong clear halo between 56-72 kDa in addition to another band located 76-102 kDa for gelatinase and one major band around 38 kDa for fibrinogenolytic enzyme respectively. The electrophorectc profile of our venom demonstrated at least one protein band between 24-31 kDa like previous reports and another two bands between 52-76 kDa and below 17 kDa stemmed probably due to the effect of natural selection in one species. According to our results Razi institute antivenin could neutralize in-vitro effects of gelatinase enzyme comprehensively. The electrophoretic profile of Iranian commercial antivenom as the main intravenous treatment of envenomed patients showed impurities in addition to F (abʹ)2 weighing 96 kDa in SDS-PAGE analysis. It proposes more efforts for refinement to avoid short and long unwanted effects in envenomed patients.
  • Keywords
    Gelatinase , Antivenom , Zymography , Echis carinatus
  • Journal title
    Astroparticle Physics
  • Serial Year
    2017
  • Record number

    2416458