Enzymatic Analysis of Iranian Echis carinatus Venom Using Zymography

Authors

  • Euikyung Kim Department of Pharmacology and Toxicology, College of Veterinary Medicine, Gyeongsang National University, Jinju, South Korea.
  • Mostafa Kamyab Faculty of Biological Sciences, Shahid Beheshti University, Tehran, Iran.
  • Ramin Seyedian Department of Pharmacology and Toxicology, Bushehr University of Medical Sciences, Bushehr, Iran.
  • Seyed Mehdi Hoseiny Department of Pharmacology and Toxicology, Bushehr University of Medical Sciences, Bushehr, Iran.
Abstract:

Snakebite is a common problem especially in tropical areas all over the world includingIran. Echis carinatus as one of the most dangerous Iranian snakes is spreading in this countryexcluding central and northwest provinces. In this study gelatinase and fibrinogenolyticproperties as two disintegrating matrix metalloproteinase enzymes were evaluated by a strongclear halo between 56-72 kDa in addition to another band located 76-102 kDa for gelatinase andone major band around 38 kDa for fibrinogenolytic enzyme respectively. The electrophorectcprofile of our venom demonstrated at least one protein band between 24-31 kDa like previousreports and another two bands between 52-76 kDa and below 17 kDa stemmed probably due tothe effect of natural selection in one species. According to our results Razi institute antivenincould neutralize in-vitro effects of gelatinase enzyme comprehensively. The electrophoreticprofile of Iranian commercial antivenom as the main intravenous treatment of envenomedpatients showed impurities in addition to F (abʹ)2 weighing 96 kDa in SDS-PAGE analysis. Itproposes more efforts for refinement to avoid short and long unwanted effects in envenomedpatients.

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Journal title

volume 16  issue 3

pages  1155- 1160

publication date 2017-07-01

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