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Solubilization of a protein synthesis inhibitor from vaccinia virions
- Source :
- Journal of virology. 45(1)
- Publication Year :
- 1983
-
Abstract
- The protein synthesis inhibitor previously demonstrated to be associated with vaccinia cores was quantitatively solubilized from vaccinia virions or cores after an endogenous protein kinase reaction at pH 10. The presence of the inhibitor in the soluble extract correlated with the presence of soluble virion proteins phosphorylated in vitro. Partially purified inhibitor blocked methionyl-tRNAfMet-40S initiation complex formation, as was the case in cell-free extracts derived from vaccinia virus-infected cells.
- Subjects :
- RNA, Transfer, Met
viruses
Immunology
Endogeny
Vaccinia virus
Biology
RNA, Transfer, Amino Acyl
Microbiology
Ribosome
chemistry.chemical_compound
Viral Proteins
Virology
Protein biosynthesis
Phosphorylation
Protein kinase A
Peptide Chain Initiation, Translational
Protein synthesis inhibitor
Virion
Hydrogen-Ion Concentration
Molecular biology
In vitro
Biochemistry
chemistry
Solubility
Insect Science
Protein Biosynthesis
Vaccinia
Protein Kinases
Ribosomes
Research Article
Subjects
Details
- ISSN :
- 0022538X
- Volume :
- 45
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Journal of virology
- Accession number :
- edsair.doi.dedup.....57e5ba6ffa13769329bc6d841a30ca88