Single major polypeptide of a calicivirus: characterization by polyacrylamide gel electrophoresis and stabilization of virions by cross-linking with dimethyl suberimidate
| Autor: | M E Soergel, F L Schaffer |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Dimethyl Suberimidate
Immunology Picornaviridae Microbiology Viral Proteins chemistry.chemical_compound Virology Animals Bovine serum albumin Sodium dodecyl sulfate Polyacrylamide gel electrophoresis Gel electrophoresis biology Molecular mass Calicivirus Molecular biology Caniformia Molecular Weight Electrophoresis chemistry Insect Science biology.protein Electrophoresis Polyacrylamide Gel Peptides Research Article |
| Zdroj: | Journal of Virology. 19:925-931 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.19.3.925-931.1976 |
| Popis: | A calicivirus, San Miguel sea lion virus serotype 4, isolate 15FT, externally labelled with 125I, was shown by gel electrophoresis to possess a single major polypeptide. The polypeptide migrated anomalously upon electrophoresis in two sodium dodecyl sulfate (SDS) systems: more slowly than bovine serum albumin in a continuous phosphate-buffered system and more rapidly than bovine serum albumin in a discontinuous system. Estimated molecular weights in the two systems were approximately 71,000 and 64,000, respectively. There was no clear evidence for a minor virion polypeptide. Treatment of purified San Miguel sea lion virions with dimethyl suberimidate, a cross-linking reagent, preserved virion integrity during long-term storage at 4 degrees C. Oligomeric species of the polypeptide were observed upon electrophoresis of products from cross-linked virions. Based upon a preferred polypeptide molecular weight estimate of 71,000 and distribution of oligomeric species, a calicivirion model with 120 monomeric protein units is proposed as an alternative to a 180-unit model. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|