| pubmed-article:4712965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C0042760 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C0042214 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:4712965 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:4712965 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:4712965 | pubmed:dateCreated | 1973-8-22 | lld:pubmed |
| pubmed-article:4712965 | pubmed:abstractText | The recent discovery of a protein kinase activity in vaccinia virions led us to search for a viral protein which is phosphorylated in vivo. Vaccinia virus was radioactively labeled by infecting cells in the presence of (32)P(1). A phosphoprotein was isolated from purified delipidated virions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The phosphoprotein appeared to be a specific viral component induced after infection. More than 60% of the phosphoprotein was associated with viral cores. The electrophoretic mobility of the protein suggested that it has a molecular weight of 11,000 to 12,000. Phosphoserine was liberated by acid hydrolysis and identified by electrophoresis with known standards. Tryptic digests of the purified phosphoprotein were analyzed by two-dimensional electrophoresis and chromatography on thin-layer cellulose plates, and a single major phosphopeptide was resolved. The high selectivity of phosphorylation suggested that the process has a specific function. | lld:pubmed |
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| pubmed-article:4712965 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:4712965 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4712965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4712965 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:4712965 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:4712965 | pubmed:author | pubmed-author:MossBB | lld:pubmed |
| pubmed-article:4712965 | pubmed:author | pubmed-author:RosemondHH | lld:pubmed |
| pubmed-article:4712965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4712965 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:4712965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4712965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4712965 | pubmed:pagination | 961-70 | lld:pubmed |
| pubmed-article:4712965 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:4712965 | pubmed:year | 1973 | lld:pubmed |
| pubmed-article:4712965 | pubmed:articleTitle | Phosphoprotein component of vaccinia virions. | lld:pubmed |
| pubmed-article:4712965 | pubmed:publicationType | Journal Article | lld:pubmed |
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