pubmed-article:4632165 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:4632165 | lifeskim:mentions | umls-concept:C0524833 | lld:lifeskim |
pubmed-article:4632165 | lifeskim:mentions | umls-concept:C0035553 | lld:lifeskim |
pubmed-article:4632165 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
pubmed-article:4632165 | lifeskim:mentions | umls-concept:C0035552 | lld:lifeskim |
pubmed-article:4632165 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:4632165 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:4632165 | pubmed:dateCreated | 1973-5-3 | lld:pubmed |
pubmed-article:4632165 | pubmed:abstractText | 1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K(+) and 0.1m-Mg(2+), were extracted with low-ionic-strength buffer 75-80% of the 30S proteins and 60-65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li(+)-EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%). | lld:pubmed |
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pubmed-article:4632165 | pubmed:language | eng | lld:pubmed |
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pubmed-article:4632165 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:4632165 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:4632165 | pubmed:month | Nov | lld:pubmed |
pubmed-article:4632165 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:4632165 | pubmed:author | pubmed-author:MathesonA TAT | lld:pubmed |
pubmed-article:4632165 | pubmed:author | pubmed-author:YaguchiMM | lld:pubmed |
pubmed-article:4632165 | pubmed:author | pubmed-author:VisentinL PLP | lld:pubmed |
pubmed-article:4632165 | pubmed:author | pubmed-author:ChouEE | lld:pubmed |
pubmed-article:4632165 | pubmed:author | pubmed-author:RollinFF | lld:pubmed |
pubmed-article:4632165 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:4632165 | pubmed:volume | 130 | lld:pubmed |
pubmed-article:4632165 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:4632165 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:4632165 | pubmed:pagination | 103-10 | lld:pubmed |
pubmed-article:4632165 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:4632165 | pubmed:year | 1972 | lld:pubmed |
pubmed-article:4632165 | pubmed:articleTitle | Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid. | lld:pubmed |
pubmed-article:4632165 | pubmed:publicationType | Journal Article | lld:pubmed |
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