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Amino acid sequence of VlF: identification in the C-terminal domain of residues common to non-hemorrhagic metalloproteinases from snake venoms.

Abstract : The complete amino acid sequence of a non-hemorrhagic fibrino(geno)lytic enzyme (VlF) isolated from Vipera lebetina venom has been determined. VlF was subjected to separate enzymatic and chemical digestions. Resulting fragments were purified by RP-HPLC and subjected for sequencing by automated Edman degradation. The amino terminus of VlF was determined by mass spectrometry. VlF was shown to be composed of 202 residues having a relative molecular mass of 22,826 Da and containing a zinc-binding site and a catalytically active residue. It displayed significant sequence similarities with many other mature metalloproteinases reported from snake venoms. Sequence comparison of hemorrhagic and non-hemorrhagic mature metalloproteinases revealed the presence at the C-terminal part of the enzymes of two residues common to only hemorrhagic metalloproteinases and two others shared by only non-hemorrhagic ones.
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Submitted on : Tuesday, January 15, 2019 - 3:37:31 PM
Last modification on : Friday, July 19, 2019 - 3:53:56 PM

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Ammar Gasmi, Najet Srairi, Habib Karoui, Mohamed El Ayeb. Amino acid sequence of VlF: identification in the C-terminal domain of residues common to non-hemorrhagic metalloproteinases from snake venoms.. BBA - Biochimica et Biophysica Acta, Elsevier, 2000, 1481 (1), pp.209-212. ⟨10.1016/s0167-4838(00)00128-x⟩. ⟨pasteur-01982311⟩

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