Linked Life Data

6319127

Source:http://linkedlifedata.com/resource/pubmed/id/6319127

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-3-1
pubmed:abstractText
Cyclic-AMP-dependent protein kinase is activated through the dissociation of active catalytic subunits from a regulatory dimer. The regulatory subunit consists of four cyclic-AMP-binding sites and two binding sites for catalytic subunits. Under well defined experimental conditions, protein kinase activation obeys apparent positive cooperativity and is linearly coupled to cyclic AMP binding. The simulation of theoretical models is used for testing working hypotheses. Here we demonstrate that the proposed stoichiometry of protein kinase activation may account for the experimentally observed properties of the system. The restrictive conditions under which theory and experimental observations are compatible are: (1) functional dependence between the two monomers of the regulatory dimer, (2) the only complexes which can accumulate at equilibrium in the considered conditions are R2C2, (cyclic AMP)2R2C and (cyclic AMP)4R2 (where R and C are the regulatory and catalytic subunits of protein kinase). An experimental procedure is proposed in order to check the validity of the theoretical predictions. The determination of the sequence of events leading to activation or inactivation of protein kinase is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
137
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
581-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
On the interactions of adenosine 3',5'-monophosphate with the components of protein kinase I. A theoretical equilibrium analysis.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't