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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1986-8-14
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pubmed:abstractText |
The 24-kDa cap binding protein (CBP) from uninfected, mock-infected and poliovirus-infected HeLa cell extracts was isolated by m7GTP affinity chromatography and examined by isoelectric focusing followed by SDS-PAGE. Two major species (pI 6.7 and 7.1) and two minor species (pI 6.5 and 6.8) were found in all cases. Preparations from postribosomal supernate (S200) and the supernate from 0.5 M KCl washed ribosomes (RSW) also demonstrated these same four species. We conclude that there are no detectable differences between ribosome-associated and soluble 24-kDa CBP and that the 24-kDa CBP is not detectably altered by poliovirus infection. We also report the presence of a previously undescribed 16-kDa polypeptide(s) doublet that copurifies with the 24-kDa CBP from uninfected, mock-infected and poliovirus-infected HeLa cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
152
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
497-501
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3014728-Carrier Proteins,
pubmed-meshheading:3014728-Chromatography, Affinity,
pubmed-meshheading:3014728-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3014728-HeLa Cells,
pubmed-meshheading:3014728-Humans,
pubmed-meshheading:3014728-Isoelectric Focusing,
pubmed-meshheading:3014728-Isoelectric Point,
pubmed-meshheading:3014728-Molecular Weight,
pubmed-meshheading:3014728-Poliovirus,
pubmed-meshheading:3014728-RNA Cap-Binding Proteins,
pubmed-meshheading:3014728-Ribosomes
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pubmed:year |
1986
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pubmed:articleTitle |
Two-dimensional gel analyses of the 24-kDa cap binding protein from poliovirus-infected and uninfected HeLa cells.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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