rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
1983-8-11
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-1187350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-1257053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-164245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-167964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-190593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-249313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-291001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-360213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-363143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-424309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-4601537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-4662103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-4850501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-4909652,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-5677314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-6165359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-6280714,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-6348877,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/6553233-791362
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0305-1048
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
11
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4257-72
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6553233-Animals,
pubmed-meshheading:6553233-Aspartate-tRNA Ligase,
pubmed-meshheading:6553233-Base Sequence,
pubmed-meshheading:6553233-Cell Line,
pubmed-meshheading:6553233-Female,
pubmed-meshheading:6553233-Guanine,
pubmed-meshheading:6553233-Humans,
pubmed-meshheading:6553233-Kinetics,
pubmed-meshheading:6553233-Lung Neoplasms,
pubmed-meshheading:6553233-Mice,
pubmed-meshheading:6553233-Ovarian Neoplasms,
pubmed-meshheading:6553233-RNA, Transfer, Amino Acyl
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pubmed:year |
1983
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pubmed:articleTitle |
The role of queuine in the aminoacylation of mammalian aspartate transfer RNAs.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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