Linked Life Data

2737204

Source:http://linkedlifedata.com/resource/pubmed/id/2737204

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-8-4
pubmed:abstractText
The N-terminal p17gag protein of the human immunodeficiency virus has been shown to incorporate radioactivity following labelling of infected cell lines with [3H]myristic acid. We investigated p17gag to determine whether the incorporated radioactivity was the consequence of N-terminal myristoylation. The virus was purified by density gradient centrifugation after labelling chronically infected H9 cells with [3H]myristic acid. The p17gag was isolated by immunoprecipitation and subjected to partial acid hydrolysis. [3H]Myristoylglycine generated by the hydrolysis was derivatized to 4-(p-nitrobenzylidene)-2-tridecanoyloxazol-5-one and identified against a co-eluting, derivatized, unlabelled N-myristoylglycine standard by reverse-phase high-performance liquid chromatography. This study unequivocally demonstrates that p17gag is an N-myristoylated protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
182
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein.
pubmed:affiliation
Division of Cancer Treatment, National Cancer Institute, Bethesda, MD 20892.
pubmed:publicationType
Journal Article