pubmed-article:6553233 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C0085845 | lld:lifeskim |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C1450029 | lld:lifeskim |
pubmed-article:6553233 | lifeskim:mentions | umls-concept:C0072841 | lld:lifeskim |
pubmed-article:6553233 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:6553233 | pubmed:dateCreated | 1983-8-11 | lld:pubmed |
pubmed-article:6553233 | pubmed:abstractText | Can a queuine-specific tRNA function normally without replacement of G by Q in its structure? To answer this, kinetics of aspartate queuine-containing tRNA (Q-tRNA) is compared with its queuine-deficient counterpart (G-tRNA). The results indicate that Asp Q-tRNA is a more effective substrate than the Asp G-tRNA. The Asp Q-tRNA exhibits a higher reaction velocity (Vmax greater than 30%) and a higher reaction rate (Km less than 55%) than its counterpart. The Asp tRNAs derived from human tumor lines and grown in athymic mice contain a full complement of queuine. This tumor tRNA exhibits aminoacylation kinetics similar to a normal liver tRNA. Reasons for observing the lack of a G-to-Q modification in cancer tRNAs by others are hypothesized. Two purified Asp isoacceptors from liver are compared for the aminoacylation reaction; small differences are noted in the Vmax, but none in the Km values. | lld:pubmed |
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pubmed-article:6553233 | pubmed:language | eng | lld:pubmed |
pubmed-article:6553233 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6553233 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6553233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:6553233 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6553233 | pubmed:month | Jun | lld:pubmed |
pubmed-article:6553233 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:6553233 | pubmed:author | pubmed-author:SinghalR PRP | lld:pubmed |
pubmed-article:6553233 | pubmed:author | pubmed-author:VakhariaV NVN | lld:pubmed |
pubmed-article:6553233 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6553233 | pubmed:day | 25 | lld:pubmed |
pubmed-article:6553233 | pubmed:volume | 11 | lld:pubmed |
pubmed-article:6553233 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6553233 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6553233 | pubmed:pagination | 4257-72 | lld:pubmed |
pubmed-article:6553233 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:6553233 | pubmed:year | 1983 | lld:pubmed |
pubmed-article:6553233 | pubmed:articleTitle | The role of queuine in the aminoacylation of mammalian aspartate transfer RNAs. | lld:pubmed |
pubmed-article:6553233 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6553233 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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