Linked Life Data

6790546

Source:http://linkedlifedata.com/resource/pubmed/id/6790546

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1981-10-29
pubmed:abstractText
A protein kinase from rabbit reticulocytes, able to phosphorylate the beta subunit of eukaryotic initiation factor 2 (eIF-2), has been demonstrated to phosphorylate also glycogen synthase. A glycogen synthase kinase (PC0.7) from rabbit skeletal muscle has been shown to phosphorylate the beta subunit of eIF-2. Comparison of highly purified preparations of the two protein kinases has indicated several similarities of properties. 1) Both enzymes were associated with two major polypeptide species, alpha (Mr = 43,000) and beta (Mr = 25,000), and exhibited apparent native molecular weights of 176,000-180,000 by gel filtration and 130,000-140,000 by sucrose density gradient sedimentation. 2) Both enzymes phosphorylated glycogen synthase, eIF-2 beta, phosvitin, and casein and were effective in utilizing GTP and ATP as phosphoryl donors. 3) Both enzymes displayed the same chromatographic behavior on phosvitin-Sepharose, phosphocellulose, and DEAE-cellulose. 4) Both enzymes underwent an autophosphorylation of the beta polypeptide when incubated with ATP and Mg2+. On the basis of these and other properties, we propose that the two protein kinases, if not identical, are very similar enzymes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8871-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Phosphorylation of glycogen synthase and of the beta subunit of eukaryotic initiation factor two by a common protein kinase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't