Abstract
A novel non-hemorrhagic basic metalloprotease, rubelase, was isolated from the venom of Crotalus ruber ruber. Rubelase hydrolyzes succinyl-L-alanyl-L-alanyl-L-alanyl p-nitroanilide (STANA), a specific substrate for elastase, and the hydrolytic activity was inhibited by chelating agents. It also hydrolyzes collagen and fibrinogen. However, hemorrhagic activity was not observed. By ESI/Q-TOF and MALDI/TOF mass spectrometry combined with Edman sequencing procedure, the molecular mass of rubelase was determined to be 23,266 Da. Although its primary structure was similar to rubelysin (HT-2), a hemorrhagic metalloprotease isolated from the same snake venom, the circumstances surrounding putative zinc binding domain HEXXHXXGXXH were found to be different when the three-dimensional computer models of both metalloproteases were compared. The cytotoxic effects of rubelase and rubelysin on cultured endothelial and smooth muscle cells were also different, indicating that the substitution of several amino acid residues causes the changes of active-site conformation and cell preference.
Highlights
Many kinds of enzymes and biologically active peptides are present in snake venoms
The primary structures of various hemorrhagic toxins have been determined [10,11,12,13,14,15,16,17] and crystal structures of some low molecular weight toxins have been reported [18,19,20,21,22,23]. These toxins have been categorized as snake venom metalloproteases (SVMPs), and classified as members of ADAMs proteins [24,25]
We report the isolation and biochemical characterization of novel non-hemorrhagic elastase from the venom of Crotalus r. ruber
Summary
Many kinds of enzymes and biologically active peptides are present in snake venoms. Hemorrhage is one of the characteristic symptoms associated with Viperidae snake envenomation. Several investigators have reported the purification, characterization, and structure of hemorrhagic principles from the venom of Protobothrops flavoviridis [3], Protobothrops mucrosquamatus [4], Deinagkistrodon acutus [5], Crotalus atrox [6,7], Crotalus ruber ruber [8] and Agkistrodon bilineatus [9]. These investigators demonstrated that these hemorrhagic toxins have proteolytic activity capable of hydrolyzing the oxidized insulin B chain, fibrinogen, glucagon, and hide powder azure. We report the isolation and biochemical characterization of novel non-hemorrhagic elastase from the venom of Crotalus r. ruber
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