Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY
Volume 150, Issue 2, Pages 285-290Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpc.2009.05.008
Keywords
Cerastes cerastes; Hemorrhage; Metalloproteinase; Proteolytic; Snake venom
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Snake venoms contain metalloproteinases that contribute to the local effects observed after envenoming. In this study, a hemorrhagic metalloproteinase (CcH1) was purified from Cerastes cerastes venom by a combination of gel filtration, ion exchange, affinity and RP-HPLC chromatography. The hemorrhagin was homogeneous on SDS-PAGE, with a molecular mass of 25 kDa. Isoelectric focusing revealed a pl of 5.5. CcH1 displayed hemorrhagic and proteolytic activities, but no esterolytic activity. The hemorrhagic and proteolytic activities of CcH1 were inhibited by EDTA and 1,10-phenanthroline, but not by PMSF, suggesting that this protein is a zinc-metalloproteinase. Furthermore, the hemorrhagic and proteolytic activities of CcH1 were stable in solution at up to 40 degrees C, with a loss of activity at >= 70 degrees C. The molecular mass and the inhibition assays suggest that the metalloproteinase CcH1 belongs to class P-I of SVMPs. (C) 2009 Elsevier Inc. All rights reserved.
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