A Preliminary Study for the Detection of Gelatinolytic Proteases from the Scorpion Androctonus crassicauda (Turkish Black Scorpion) Venom
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Objectives: Despite the long history on proteolytic activity studies, no study has been reported about the presence of proteases from the Turkish scorpion A. crassicauda venom which is among the most toxic species in the world. The present work is a preliminary study indicating the presence of gelatinolytic proteases in the A. crassicauda crude venom which almost nothing is known about its components. Methods: Protein contents of the venom were analyzed by electrophoresis. Further, the venom fractions were separated by liquid chromatography. Proteolytic activities of crude venom and each fraction were determined by zymogram assay. Results: Two proteins with gelatinolytic activity were detected between 36-45 kDa and 97-116 kDa in the soluble venom at a range of pH 4.0 to 8.0. Proteolytic bands from the fractions obtained chromatographically were detected as three bands between 14.2 and 20 kDa; one band between 20 and 24 kDa; three bands between 24 and 29 kDa; two bands between 97 and 116 kDa at pH 7. Conclusion: Here, first electrophoretic separation of the venom from A. crassicauda where the proteolytic activity against gelatin is reported. These enzymes may prove to be a useful tool for the study of toxin processing and understanding the mechanism of venom activation.