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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
|
| pubmed:dateCreated |
1983-3-11
|
| pubmed:abstractText |
Using ethanol-salt extraction and ion-exchange chromatography, an acid protein was isolated from 80S pea ribosomes. The protein is localized in the large subunit, is phosphorylated and has a molecular weight of 14000 and pI of 4.7. These features and the results of a comparative study of tryptic hydrolysates of the plant protein and of the protein under study suggest that the latter is homologous to the ribosomal protein L7/L12 of a prokaryotic type.
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0320-9725
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
47
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1899-906
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading | |
| pubmed:year |
1982
|
| pubmed:articleTitle |
[Acid proteins of eukaryotic cell ribosomes. Isolation of the protein similar to E. coli L7/L12 from 80S pea ribosomes].
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
English Abstract
|