Amino acid sequence of VlF: identification in the C-terminal domain of residues common to non-hemorrhagic metalloproteinases from snake venoms.
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.
Gasmi
A
A
Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, B.P. 74, 1002, Tunis-Belvédère, Tunisia. ammar.gasmi@pasteur.rns.tn
Srairi
N
N
Karoui
H
H
El Ayeb
M
M
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*
D005343:Fibrinolytic Agents; D014757:Viper Venoms; D008666:Metalloendopeptidases