pubmed-article:7215342 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C0596973 | lld:lifeskim |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:7215342 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
pubmed-article:7215342 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:7215342 | pubmed:dateCreated | 1981-6-23 | lld:pubmed |
pubmed-article:7215342 | pubmed:abstractText | The pulse-chase experiments with Friend erythroleukemia cells designed to reveal the metabolic properties of the protein complex of 40-S particles showed that the major polypeptides of this complex turn over with half-lives between 19 h and 206 h. the main conclusion from the experiments is that the complex does not degrade as a single unit. Since the individual polypeptides forming the complex live much longer than hnRNA, and in addition degrade at a different rate, we considered the following two modes of degradation as most likely. (1) The complex might not be subjected to a profound degradation at the end of the processing of associated pre-mRNA. In this case it should exist as a long-lived recyclable mosaic of metabolically differing polypeptides whose replacement takes place at a specific rate. (2) Alternatively, the protein complex might be completely degraded at the end of processing, but in a way that liberates free individual polypeptides available for recycling. The further experiments indicate that the 37 000-Mr, 34 000-Mr and 32 000-Mr core proteins in isolated 40-S particles and in particles associated with a nuclear fraction released from chromatin after micrococcal nuclease digestion degrade at different rates. These experiments suggest the existence of at least a metabolic heterogeneity among the population of nuclear particles carrying pre-mRNA. | lld:pubmed |
pubmed-article:7215342 | pubmed:language | eng | lld:pubmed |
pubmed-article:7215342 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7215342 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7215342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7215342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7215342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7215342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7215342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7215342 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7215342 | pubmed:month | Jan | lld:pubmed |
pubmed-article:7215342 | pubmed:issn | 0014-2956 | lld:pubmed |
pubmed-article:7215342 | pubmed:author | pubmed-author:IvanovaEE | lld:pubmed |
pubmed-article:7215342 | pubmed:author | pubmed-author:DjondjurovLL | lld:pubmed |
pubmed-article:7215342 | pubmed:author | pubmed-author:PironchevaGG | lld:pubmed |
pubmed-article:7215342 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7215342 | pubmed:volume | 113 | lld:pubmed |
pubmed-article:7215342 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7215342 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7215342 | pubmed:pagination | 569-73 | lld:pubmed |
pubmed-article:7215342 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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pubmed-article:7215342 | pubmed:year | 1981 | lld:pubmed |
pubmed-article:7215342 | pubmed:articleTitle | Turnover of the major polypeptides of 40-S monomer particles. | lld:pubmed |
pubmed-article:7215342 | pubmed:publicationType | Journal Article | lld:pubmed |
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