Linked Life Data

179457

Source:http://linkedlifedata.com/resource/pubmed/id/179457

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-8-2
pubmed:abstractText
Ribonucleic acid from TMV and BMV can accept AMP and CMP when digested with VPD. This incorporation is catalyzed by E. coli and yeast tRNA nucleotidyl transferases. Complex formation is obtained between TYMV RNA and tRNA nucleotidyl transferase in sucrose gradients while TMV and BMV RNAs failed to form a complex in the same conditions. The affinity of the enzyme for viral RNAs is lower than the affinity for tRNA as shown by complex formation on nitrocellulose filters and competition with tRNA. Coat protein from TMV particles enhances AMP and CMP incorporation onto tRNA catalyzed by the E. coli tRNA nucleotidyl transferase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0300-5410
pubmed:author
pubmed:issnType
Print
pubmed:volume
127A
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-46
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Interactions of plant viral RNAs and tRNA nucleotidyl transferase.
pubmed:publicationType
Journal Article