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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1977-12-29
|
| pubmed:abstractText |
The polypeptides of polyoma and SV40 virions are phosphorylated. An estimate of the amount of phosphorylation of the major virus capsid protein (VPI) has been made using two-dimensional gel electrophoresis to resolve phosphorylated from non-phosphorylated forms. The results suggest that in both polyoma and SV40 virions about 12% of VPI molecules are phosphorylated. In unassembled VPI molecules immunoprecipitated from extracts of infected cells the proportion is greater, about 33%. The possibility that phosphorylated VPI may form the penton proteins of the virus capsid is discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0022-1317
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
37
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
75-83
|
| pubmed:dateRevised |
2001-11-2
|
| pubmed:meshHeading | |
| pubmed:year |
1977
|
| pubmed:articleTitle |
Phophorylation of polyoma and SV40 virus proteins.
|
| pubmed:publicationType |
Journal Article
|