Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1979-8-16
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.
pubmed:language
eng
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
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5350-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Disassembly and gross structure of particulate aminoacyl-tRNA synthetases from rat liver. Isolation and the structural relationship of synthetase complexes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.