Amino acid sequence of a phospholipase A2 from the venom of Trimeresurus gramineus (green habu snake)
| Autor: | Hiroko Nakamura, Shunji Sakamoto, Chun-Chang Chang, Song-Yuan Liu, Motonori Ohno, Hiroshi Kihara, Naoko Oda |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Phospholipase A
Clostripain Chymotrypsin biology Molecular Sequence Data Molecular Conformation Snakes Toxicology biology.organism_classification Phospholipases A Phospholipases A2 Phospholipase A2 Trimeresurus gramineus Biochemistry Crotalid Venoms biology.protein Animals Amino Acid Sequence Binding site Tyrosine Peptide sequence Chromatography High Pressure Liquid |
| Zdroj: | Toxicon. 29:157-166 |
| ISSN: | 0041-0101 |
| DOI: | 10.1016/0041-0101(91)90100-6 |
| Popis: | Two phospholipases A 2 , named phospholipases A 2 -I and A 2 -II, were purified to homogeneity from the venom of Trimeresurus gramineus (green habu snake). The complete amino acid sequence of phospholipase A 2 -I was determined by sequencing the native protein and the peptides produced by enzymatic ( Achromobacter protease I, clostripain, and chymotrypsin) and chemical (hydroxylamine) cleavages of the S -pyridylethylated derivative of the protein. The protein consisted of 122 amino acid residues and was similar in sequence to phospholipases A 2 from the venoms of crotalid snakes which belong to the category of Group II. A most striking feature of this protein is that tyrosine at the 28th position which is common in phospholipases A 2 and is assumed to be a part of the Ca 2+ -binding loop is replaced by phenylalanine. Such replacement is the first finding in Group II phospholipases A 2 . Secondary structure compositions of phospholipase A 2 -I are similar to those of Crotalus atrox phospholipase A 2 . No appreciable Ca 2+ -induced difference spectrum was observed, due probably to the absence of the effective chromophoric groups in the neighborhood of the Ca 2+ binding site although Ca 2+ is bound with affinity similar to that for T. flavoviridis phospholipase A 2 . |
| Databáze: | OpenAIRE |
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