Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
1983-6-23
pubmed:abstractText
The 58000 dalton (58K) protein coded for by early region 1B of human adenovirus type 5 (Ad5) was found to be phosphorylated. At least three major tryptic phosphopeptides were identified and the average number of phosphates per 58K molecule was estimated to be between two and three. Thus, it was possible that each phosphopeptide contained just one phosphate group. The ratio of phosphoserine to phosphothreonine was about 2 to 1 on average and essentially no phosphotyrosine was detected. No evidence was found to suggest that cAMP-dependent protein kinase was involved in the phosphorylation of 58K. Previous studies have shown that 58K was phosphorylated when immunoprecipitates containing Ad5 early region 1 proteins were incubated in vitro with [gamma-32P]ATP. Analysis of the phosphopeptides of 58K labelled under these conditions indicated a large number of phosphorylation sites which differed from those found in vivo. Thus, the action of kinases in the in vitro phosphorylation of 58K in immunoprecipitates did not mimic the enzymic activity responsible for 58K phosphorylation in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1069-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Studies on the phosphorylation of the 58000 dalton early region 1B protein of human adenovirus type 5.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't