Structural components of mouse mammary tumor virus. II. Isolation and purification of virion polypeptides
| Autor: | Mary Jane Yagi, B H Robertson, R E Stutzman, Richard W. Compans |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Antigenicity
Immunogen animal structures viruses Immunology Detergents Immunoelectrophoresis Biology Microbiology Virus Viral Proteins Virology medicine Antigens Viral Glycoproteins Antiserum Gel electrophoresis chemistry.chemical_classification medicine.diagnostic_test Mouse mammary tumor virus Virion Hemagglutination Inhibition Tests biology.organism_classification Molecular biology chemistry Mammary Tumor Virus Mouse Insect Science Glycoprotein Research Article |
| Zdroj: | Journal of virology. 26(2) |
| ISSN: | 0022-538X |
| Popis: | Mouse mammary tumor virus (MMTV) glycoproteins and nonglycosylated polypeptides were purified by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Primary amino groups were labeled with fluorescamine to enable visualization of MMTV polypeptides in the gels. Protein bands were sliced from the gels and eluted with 90 to 95% recovery. Eight MMTV polypeptides, including three of the major viral components as well as five minor proteins, were routinely obtained. Double diffusion assays and immunoelectrophoresis confirmed the retention of antigenicity identical to that of untreated MMTV virions. Antisera obtained from MMTV-free BALB/c mice immunized with these purified proteins reacted with the polypeptide immunogen as well as with detergent-disrupted MMTV virions from mouse milk or cell culture. Double diffusion assays using the specific mouse antisera failed to detect any cross-reactivity among the isolated polypeptides. A hemagglutination-inhibition assay demonstrated that the ability of MMTV virions to inhibit the hemagglutinating properties of influenza virus resides in the glycosylated polypeptides gp52, gp37.7, and gp33. |
| Databáze: | OpenAIRE |
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