Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1986-2-19
pubmed:abstractText
Initiation factor 2 from adult rat brain was isolated from salt-washed microsomes using a three-step purification process consisting of heparin-Sepharose, phosphocellulose and diethylaminoethyl-cellulose (DEAE cellulose) column chromatographies. The initiation factor 2(eIF-2) was phosphorylated in subunits alpha and beta by the endogenous protein kinase activity present in the pruified preparation. This protein kinase activity proved to be mostly a casein kinase, although the possible presence of a very specific alpha kinase activity cannot be dismissed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
333-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Initiation factor 2 isolated from rat brain contains kinase activities responsible for its phosphorylation.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't