Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1988-12-14
|
pubmed:abstractText |
When the assay for the interferon-induced protein kinase is performed in the presence of ammonium sulfate, the activity of other cellular kinases is selectively inhibited. Ammonium sulfate has little effect on the autophosphorylation of the interferon-induced kinase or the phosphorylation of a secondary acceptor, calf thymus histone. Conditions are described for the measurement of interferon-induced kinase activity by trichloroacetic acid precipitation.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0003-2697
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
173
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
445-9
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading | |
pubmed:year |
1988
|
pubmed:articleTitle |
Addition of ammonium sulfate improves the specificity of the assay for the interferon-induced protein kinase.
|
pubmed:affiliation |
Department of Microbiology, School of Medicine, University of Pittsburgh, Pittsburgh 15261.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|