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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1981-4-24
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pubmed:abstractText |
Poly(A)-containing RNA from frozen adult rat brain were fractionated by centrifugation in a formamide/sucrose gradient. Individual fractions were used to program protein synthesis in vitro in a reticulocyte lysate. The cell-free translation products were analyzed by two-dimensional electrophoresis in polyacrylamide slab gels. We observed a heterodispersion of the mRNA translation activity coding for the beta-tubulin subunit which contrasts with a relatively homogeneous distribution of the alpha-tubulin subunit mRNA. These last mRNA species are present in a peak which sediments near the 18-S region of the gradient whereas the beta-tubulin mRNA activity is predominant in the fractions corresponding to the heaviest mRNA species. When these heaviest RNAs were separated again by centrifugation in a second formamide/sucrose gradient, a poly(A)-rich RNA population was obtained that was enriched in RNA for programming the beta-tubulin subunit. Analysis of the products whose synthesis in vitro was directed by this mRNA population revealed that beta tubulin was the main protein formed, the ratio beta/alpha being more than tenfold greater than in the products translated in vitro using total poly(A)-rich RNA.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
112
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
601-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6161815-Animals,
pubmed-meshheading:6161815-Brain Chemistry,
pubmed-meshheading:6161815-Cell-Free System,
pubmed-meshheading:6161815-Centrifugation, Density Gradient,
pubmed-meshheading:6161815-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6161815-Poly A,
pubmed-meshheading:6161815-Protein Biosynthesis,
pubmed-meshheading:6161815-RNA,
pubmed-meshheading:6161815-RNA, Messenger,
pubmed-meshheading:6161815-Rats,
pubmed-meshheading:6161815-Reticulocytes,
pubmed-meshheading:6161815-Tubulin
|
pubmed:year |
1980
|
pubmed:articleTitle |
Partial purification of the alpha-tubulin and beta-tubulin messenger RNAs from rat brain.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|