Linked Life Data

6297892

Source:http://linkedlifedata.com/resource/pubmed/id/6297892

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-4-15
pubmed:abstractText
Total R proteins and total cAMP-dependent protein kinase activity during rat liver development reach highest values per unit DNA when the organ has attained full metabolic competence. The parallel changes indicate coordinate synthesis of R and C subunits during hepatic development. In contrast to total R2 . C2, protein kinase activation and endogenous cAMP levels were highest around birth. Immunotitration with anti-RI and anti-RII in the presence of protein-A-Sepharose of extracts obtained from various developmental stages and from hepatomas suggested a relation of both protein kinase I and II to the terminal differentiation of the organ rather than to cellular proliferation rates. The type-II enzyme appears to be subject to additional regulations connected with neonatal adaptation phenomena. A non-enzymic analysis of the protein kinase activation status is described. It is based on the determination of the ratio of amounts: R . cAMP/total R, which showed a linear correlation with the conventional protein kinase activity ratio (-cAMP/+cAMP).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-74
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Isoenzymes of cAMP-dependent protein kinase in developing rat liver and in malignant hepatic tissues.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't