title: 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.
authors.affiliation: Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, B.P. 74, 1002, Tunis-Belvédère, Tunisia. ammar.gasmi@pasteur.rns.tn
authors.forename: A
authors.initials: A
authors.lastname: Gasmi
authors.forename: N
authors.initials: N
authors.lastname: Srairi
authors.forename: H
authors.initials: H
authors.lastname: Karoui
authors.forename: M
authors.initials: M
authors.lastname: El Ayeb
mesh_terms: D000595:Amino Acid Sequence; D005343:Fibrinolytic Agents / Q000737:chemistry* / Q000302:isolation & purification; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment; D014757:Viper Venoms / Q000737:chemistry*
chemical_list: D005343:Fibrinolytic Agents; D014757:Viper Venoms; D008666:Metalloendopeptidases