Linked Life Data

6305867

Source:http://linkedlifedata.com/resource/pubmed/id/6305867

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-8-11
pubmed:abstractText
The herpes simplex virus(HSV)-coded thymidine kinase (TK) enzyme complex was isolated from HSV type 1 strain Lennette(TK+)-infected CLID (TK-) cells and was enriched by streptomycin sulfate and ammonium sulfate fractionation. This enzyme preparation was tested for dTMP:Ado (adenosine) and for dTMP:ADP phosphotransferase activities. The presence of dTMP:Ado phosphotransferase activity was proven by time-course studies with cells infected for 0-18 h, by biophysical studies in polyacrylamide gels, by affinity chromatography studies using AMP- and dTMP-Sepharose, and by immuno-neutralization experiments. The presence of dTMP:ADP phosphotransferase activity was demonstrated by kinetic experiments. These results were taken as evidence that the two functional subunits of the HSV-TK enzyme complex, AMP:dThd (deoxythymidine) phosphotransferase and ATP: dThd kinase, catalyze highly reversible enzyme reactions. New data are presented indicating that the ATP:dThd kinase is a nonspecific enzyme with respect to the nucleoside acceptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-5526
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-84
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Adenosine- and ADP-phosphorylating capacity of herpes simplex virus-induced thymidine kinase enzyme complex.
pubmed:publicationType
Journal Article