The purification and characterization of a necrotoxin from tarantula, Dugesiella hentzi (Girard), venom
| Autor: | Choong K. Lee, Billy C. Ward, George V. Odell, D.E. Howell, Tak K. Chan |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Insecta
Time Factors Arginine Biophysics Venom Biology Biochemistry chemistry.chemical_compound Mice Animals Amino Acids Molecular Biology Polyacrylamide gel electrophoresis Creatine Kinase Toxins Biological Methionine Binding Sites Isoelectric focusing Venoms Tryptophan Sodium Dodecyl Sulfate Spiders Succinates Hydrogen-Ion Concentration Chromatography Ion Exchange Electrophoresis Disc Molecular biology Molecular Weight Isoelectric point chemistry Chromatography Gel Biological Assay Electrophoresis Polyacrylamide Gel Female Spectrophotometry Ultraviolet Isoelectric Focusing Cysteine Protein Binding |
| Zdroj: | Archives of biochemistry and biophysics. 164(1) |
| ISSN: | 0003-9861 |
| Popis: | The major toxin, a necrotoxin, of the venom of Dugesiella hentzi (Girard) has been purified by gel filtration. The purified toxin was homogeneous by gel filtration, polyacrylamide gel electrophoresis, and an isoelectric focusing procedure. The molecular weight estimation was 6700 and the isoelectric pH was 10.0. The amino acid composition shows 16 lysine, 8 cysteine, and one tryptophan residues, with no tyrosine, methionine, alanine, arginine, or histidine residues. The purified protein is toxic to certain insects and mice with the primary site of action being muscle tissue in the mouse. Modification of the single tryptophan residue resulted in a loss of toxicity. A significant increase of serum creatine phosphokinase activity was observed in mice injected with the necrotoxin. Histological examination showed the primary lesions were acute focal areas of myocardial necrosis, and no histological differences in myocardial lesions were seen between mice injected with the purified necrotoxin or with the whole venom. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|