Some chemical properties of the venom of the rattlesnake, Crotalus viridis helleri
| Autor: | Nobuo Tamiya, Findlay E. Russell, T.R. Pattabhiraman, Nobuyo Maeda |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
chemistry.chemical_classification
Chromatography Chemical Phenomena biology Hydrolysis Size-exclusion chromatography Ion chromatography Crotalus Peptide Toxicology biology.organism_classification Amino acid Lethal Dose 50 Crotamine Chemistry Mice chemistry Sephadex Crotalid Venoms Chromatography Gel Animals Electrophoresis Polyacrylamide Gel Amino Acids Peptides Polyacrylamide gel electrophoresis |
| Zdroj: | Toxicon. 16:431-441 |
| ISSN: | 0041-0101 |
| DOI: | 10.1016/0041-0101(78)90140-x |
| Popis: | The venom of the Southern Pacific Rattlesnake, Crotalus viridis helleri, was separated into three lethal and several non-lethal peaks by gel filtration. Peak I was a protein having a mol. wt of ca. 100,000 and an intravenous ld 50 of 0.58 mg/kg. Peak II had a mol. wt of ca. 30,000 and a ld 50 of 1·7 mg/kg. Peak III, the peptide, had a mol. wt of ca. 6000 and a ld 50 of 1·96 mg/kg and moved as a cation on strip and polyacrylamide gel electrophoresis. On ion exchange chromatography the peptide was resolved into three lethal fractions. The major fraction, C, was a basic polypeptide containing 43 amino acid residues with six half cystine residues. Its mol. wt was 4990, as calculated from its sequence, 7600 as estimated from Sephadex G-50 gel filtration and 5200 by SDS- disc gel electrophoresis. The differences are being studied. Analysis showed the peptide contained almost 20% lysine. On sequencing, the most basic amino acid residues were distributed in the N-terminal and C-terminal parts. The middle part was rather hydrophobic. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|