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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
1979-8-16
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pubmed:abstractText |
The major high molecular weight complex of aminoacyl-tRNA synthetases is purified about 1000-fold with 30% yield from rat liver. The synthetase complex sediments at 24 S with a molecular weight of 900,000 +/- 75,000 and contains aminoacylation activities for lysine, arginine, isoleucine, leucine, methionine, glutamine, glutamate, and proline. The 24 S synthetase complex dissociates into 21 S, 18 S, 13 S, 12 S, and 10 S complexes with specific enzymatic activities. Dissociation of the 24 S complex into active free synthetases is achieved by hydrophobic interaction chromatography. The disassembly of the synthetase complex is consistent with the structural model of a heterotypic multienzyme complex and suggests that the complex formation is due to the specific intermolecular interactions among the synthetases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
5350-6
|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:447654-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:447654-Animals,
pubmed-meshheading:447654-Liver,
pubmed-meshheading:447654-Macromolecular Substances,
pubmed-meshheading:447654-Male,
pubmed-meshheading:447654-Molecular Weight,
pubmed-meshheading:447654-Multienzyme Complexes,
pubmed-meshheading:447654-Rats
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pubmed:year |
1979
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pubmed:articleTitle |
Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. Isolation and the structural relationship of synthetase complexes.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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