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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1981-6-23
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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.
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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/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Heterogeneous Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
113
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-73
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:7215342-Animals,
pubmed-meshheading:7215342-Cycloheximide,
pubmed-meshheading:7215342-Friend murine leukemia virus,
pubmed-meshheading:7215342-Half-Life,
pubmed-meshheading:7215342-Leukemia, Experimental,
pubmed-meshheading:7215342-Mice,
pubmed-meshheading:7215342-Molecular Weight,
pubmed-meshheading:7215342-Neoplasm Proteins,
pubmed-meshheading:7215342-Nucleoproteins,
pubmed-meshheading:7215342-Peptides,
pubmed-meshheading:7215342-RNA, Heterogeneous Nuclear,
pubmed-meshheading:7215342-RNA, Neoplasm,
pubmed-meshheading:7215342-Ribonucleoproteins
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pubmed:year |
1981
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pubmed:articleTitle |
Turnover of the major polypeptides of 40-S monomer particles.
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pubmed:publicationType |
Journal Article
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