Hinda Boukhalfa-Abib

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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(More)
Snake venom metalloproteinases (SVMPs) are the most abundant components in snake venoms. They are important in the induction of systemic alterations and local tissue damage after envenomation. CcMP-II, which is a metalloproteinase purified from Cerastes cerastes snake venom, was obtained by a combination of gel filtration, ion-exchange and affinity(More)
Snake venom metalloproteinases are the most abundant toxins in Viperidae venoms. In this study, a new hemorrhagin, Cc HSM-III (66 kDa), was purified from Cerastes cerastes venom by gel filtration, ion exchange, and reversed-phase high-performance liquid chromatographies. The analysis of Cc HSM-III by liquid chromatography with a tandem mass spectrometry(More)
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