Enzymatic Analysis of Iranian Echis carinatus Venom Using Zymography

Document Type: Research article

Authors

1 Faculty of Biological Sciences, Shahid Beheshti University, Tehran, Iran.

2 Department of Pharmacology and Toxicology, College of Veterinary Medicine, Gyeongsang National University, Jinju, South Korea.

3 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 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.

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