Linked Life Data

3396332

Source:http://linkedlifedata.com/resource/pubmed/id/3396332

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-9-7
pubmed:abstractText
1. Phosphorylation of acid-soluble chromatin proteins from thymus or liver of calf, rabbit, pig, rat, rooster and trout by purified cyclic GMP-dependent protein kinase was studied in vitro using acetic acid-urea slab gel electrophoresis and autoradiography. 2. HMG 14, histone H1 and an unknown band representing probably a proteolytic fragment of histone H1 were phosphorylated in all mammals studied. 3. In avian liver, HMG 14 showed no phosphorylation and histone H1 was replaced by a H1(0)/H5-like heavily phosphorylated protein. 4. The only 32P-acceptor in trout liver apparently belongs to the C/D-family of acid-soluble chromatin proteins. H6-protein was not phosphorylated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Phosphorylation of acid-soluble chromatin proteins from tissues of different species by purified cyclic GMP-dependent protein kinase.
pubmed:affiliation
Department of Biochemistry, University of Kuopio, Finland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't