Further evidence for multiple proteins in the foot-and-mouth disease virus particle
| Autor: | Fred Brown, J. N. Burroughs, D. V. Sangar, P. Talbot, David J. Rowlands |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Sucrose
Protein subunit Sodium Ion chromatography chemistry.chemical_element Biology Kidney Tritium Virus Cell Line Viral Proteins Aphthovirus Virology Cricetinae Culture Techniques Centrifugation Density Gradient Animals Urea Trypsin Amino Acids Uridine Gel electrophoresis Carbon Isotopes Molecular mass Staining and Labeling Sulfates Hydrogen-Ion Concentration biology.organism_classification Chromatography Ion Exchange Electrophoresis Disc Molecular biology Molecular Weight Biochemistry chemistry Cattle Foot-and-mouth disease virus Isoelectric Focusing Peptides Azo Compounds Cysteine |
| Zdroj: | The Journal of general virology. 13(1) |
| ISSN: | 0022-1317 |
| Popis: | Summary Further evidence has been obtained which confirms that foot-and-mouth disease virus contains several structural proteins. By electrophoresis in urea-polyacrylamide gels, virus of type O gave six distinct bands. In sodium dodecyl sulphate-polyacrylamide gels four proteins with molecular weights of 34, 30, 26 and 13.5 × 103 were clearly demonstrated. When virus preparations were labelled with a single amino acid, in both sodium dodecyl sulphate-polyacrylamide and urea-polyacrylamide gel electrophoresis, the fastest migrating protein contained no arginine and only traces of cysteine. This protein also stained differently from the other bands with Coomassie Blue and was absent from the 12s protein subunit prepared by mild acid (pH 6.5) disruption of the virus. This protein was separated from the 12s subunit by sucrose gradient centrifugation and by ion exchange chromatography on Amberlite IRC-50. |
| Databáze: | OpenAIRE |
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