Mason-Pfizer monkey virus: analysis and localization of virion proteins and glycoproteins.
AUTOR(ES)
Schochetman, G
RESUMO
The polypeptide composition of Mason-Pfizer monkey virus was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Six major polypeptides of molecular weights 68,000, 27,000, 20,000, 14,000, 12,000, and 10,000 were resolved regardless of the cell type (i.e., two human and two rhesus) in which the virus was grown. Protein gp68 (68,000) represented the major virus glycoprotein and protein gp20 (20,000) represented a minor glycoprotein of the virion, again regardless of the cell type of origin of the virus. Protein gp68 appears to be located on the outer surface of the viral envelope, as demonstrated by lactoperoxidase catalyzed iodination of intact virions. Additional glycoproteins were shown to be virion associated; their presence depended, however, on the cell type in which the virus was propagated.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=355720Documentos Relacionados
- RNA subunit structure of Mason-Pfizer monkey virus.
- Sialylatin of glycoproteins of murine mammary tumor virus, murine leukemia virus, and Mason-Pfizer monkey virus.
- Immunological Properties of Two Polypeptides of Mason-Pfizer Monkey Virus
- Effect of monensin on Mason-Pfizer monkey virus glycoprotein synthesis.
- Analysis of Mason-Pfizer Monkey Virus Gag Particles by Scanning Transmission Electron Microscopy
