Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
1996-7-17
pubmed:abstractText
The interaction between the bovine mitochondrial translational elongation factor Tu.Ts complex (EF-Tu.Tsmt) and aminoacyl-tRNA has been investigated using a nuclease protection assay and fluorescence enhancement of [AEDANS-s2C]Tyr-tRNA(Tyr). The equilibrium dissociation constant, Kd, for the EF-Tu.Tsmt:GTP:E. coli Phe-tRNA complex is approximately 50 nM. A similar binding constant (30 nM) is obtained using bovine mitochondrial Phe-tRNA. The equilibrium binding constant for the EF-Tu.Tsmt:GTP:yeast [AEDANS-s2C]Tyr-tRNA(Tyr) complex is approximately 4 nM when determined using the fluorescence enhancement assay.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0261-3166
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Interaction of mitochondrial elongation factors Tu.Ts with aminoacyl-tRNA.
pubmed:affiliation
University of North Carolina at Chapel Hill, Department of Chemistry 27599-3290, USA.
pubmed:publicationType
Journal Article, In Vitro