Amino acid sequence of VlF: identification in the C-terminal domain of residues common to non-hemorrhagic metalloproteinases from snake venoms
| Autor: | Habib Karoui, Mohamed El Ayeb, Ammar Gasmi, Najet Srairi |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Molecular mass Edman degradation C-terminus Molecular Sequence Data Biophysics Metalloendopeptidases Venom Viper Venoms Biology Matrix metalloproteinase Biochemistry Molecular biology Molecular Weight Residue (chemistry) Enzyme Fibrinolytic Agents chemistry Structural Biology Amino Acid Sequence Sequence Alignment Molecular Biology Peptide sequence |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1481:209-212 |
| ISSN: | 0167-4838 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect