Protein and cDNA Structures of an Acidic Phospholipase A2, the Enzymatic Part of an Unusual, Two-Component Toxin fromVipera palaestinae
| Autor: | Franc Gubenšek, Igor Krizaj, Jože Pungerčar, P Bencina, Avner Bdolah |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
DNA
Complementary Molecular Sequence Data Biophysics Viper Venoms Phospholipase Peptide Mapping Polymerase Chain Reaction Biochemistry Phospholipases A Phospholipase A2 Viperidae medicine Animals Chymotrypsin Trypsin Amino Acid Sequence Molecular Biology Peptide sequence DNA Primers chemistry.chemical_classification Base Sequence biology Molecular mass Protein primary structure Cell Biology Peptide Fragments Recombinant Proteins Amino acid Molecular Weight Phospholipases A2 chemistry biology.protein Indicators and Reagents medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 227:374-379 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1996.1515 |
| Popis: | In the venom of Vipera palaestinae an unusual, two-component toxin was found. The two components of the toxin are an acidic phospholipase A2 (VpaPLA2) and a basic protein, both with an apparent molecular mass of about 15 kDa. Each component alone is not toxic; however, their mixture is lethal. We have determined the amino acid and cDNA sequences of VpaPLA2. The protein primary structure was solved by sequencing the peptides generated by chemical cleavage of the molecule using CNBr, formic acid and hydroxylamine-hydrochloride and by enzymatic fragmentation with trypsin and chymotrypsin. VpaPLA2 consists of 122 amino acid residues and has all the structural characteristics of subgroup IIA PLA2s. It shows the highest amino acid similarity to a non-toxic phospholipase A2 from Eristocophis macmahoni (82%), whereas the most similar toxic phospholipases A2 share about 70% of residues with VpaPLA2. The substitution of His20 for a hydrophobic residue (Leu) in VpaPLA2 might be one of the reasons that its complex with the basic protein could not be observed. |
| Databáze: | OpenAIRE |
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