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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1978-9-15
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pubmed:abstractText |
Purification and partial characterization of the poliovirus RNA-linked protein (VPg) are described. VPg has been freed from the RNA by ribonuclease digestion and phenol extraction. Gel filtration chromatography of VPg-pUp (labeled with 32P) in 0.5% sodium dodecyl sulfate or 6 M guanidine HCl indicates that it has a molecular weight of about 12,000. VPg is bound to the 5' end of poliovirion RNA by a phosphodiester bond between a tyrosine residue in the VPg molecule and the 5'-terminal uridine. After acid hydrolysis of [3H]tyrosine-labeled VPg-pU, free tyrosine can be released by venom phosphodiesterase. Acid hydrolysis of VPg-p labeled with either 32P or [3H] tyrosine yields tyrosine-phosphate. There appears to be only 1 tyrosine residue per VPg molecule.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Organophosphorus Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
253
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5263-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:209034-Binding Sites,
pubmed-meshheading:209034-Molecular Weight,
pubmed-meshheading:209034-Organophosphorus Compounds,
pubmed-meshheading:209034-Poliovirus,
pubmed-meshheading:209034-Protein Binding,
pubmed-meshheading:209034-RNA, Viral,
pubmed-meshheading:209034-Ribonucleases,
pubmed-meshheading:209034-Tyrosine,
pubmed-meshheading:209034-Viral Proteins
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pubmed:year |
1978
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pubmed:articleTitle |
Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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