Concentration and purification of feline leukaemia virus (FeLV) and its outer envelope protein gp70 by aqueous two-phase systems
| Autor: | Bror Morein, Karin Malm, Sigrid Eriksson, Lena Marmstål Hammar |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
viruses
Immunoblotting Retroviridae Proteins Gene Products gag Feline leukemia virus Virus Cell Line Retrovirus Viral envelope Viral Envelope Proteins Virology Animals Centrifugation chemistry.chemical_classification biology Leukemia Virus Feline Dextran Sulfate Aqueous two-phase system Antibodies Monoclonal Dextrans Group-specific antigen biology.organism_classification Molecular biology Molecular Weight chemistry Solubility Electrophoresis Polyacrylamide Gel Glycoprotein |
| Zdroj: | Journal of virological methods. 24(1-2) |
| ISSN: | 0166-0934 |
| Popis: | The major protective antigens of retro viruses are considered to be their glycosylated envelope proteins. However, the methods commonly employed to enrich and purify virus from culture media such as pelleting and density-gradient centrifugation result in a low recovery of the viral external glycoproteins. This is an obvious drawback when the virus is intended for use in a vaccine. In search for alternative methods to concentrate and purify FeLV, we have attempted extraction in two-phase systems based on water-soluble polymers (Albertsson PA., Biochem Biophys Acta 1958; 27: 378–395). A variety of polymer systems was tested. Some of them seem attractive for a large-scale concentration of the virus and/or its glycoprotein. The distribution between the phases of two FeLV proteins, the outer envelope protein, gp70, and the gag protein, p27, was determined. With a system composed of dextran sulfate and polyvinyl alcohol both the glycoprotein and the gag protein were almost completely recovered in the lower phase which constitutes about 3% of the total system in weight. The two proteins were more than 40-fold purified as calculated on protein basis. The proteins can be extracted readily. |
| Databáze: | OpenAIRE |
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