Linked Life Data

3597418

Source:http://linkedlifedata.com/resource/pubmed/id/3597418

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1987-8-14
pubmed:abstractText
A cyclic nucleotide- and Ca2+-independent protein kinase has been identified and purified from pig liver to apparent homogeneity. This independent protein kinase is basically inactive but can be activated by a 4-min incubation with 0.25 mM ATP and 2 mM Mg2+. This ATP X Mg-mediated activation appears to involve an intramolecular autophosphorylation as it is independent of kinase concentration. Phosphoamino acid analysis further indicates that this intramolecular autophosphorylation/activation process is predominantly on a serine residue. The nonphosphorylated, inactive form of the kinase is extremely trypsin-labile, whereas the phosphorylated, active kinase is more resistant to trypsin, suggesting a conformational change during the activation process. Autophosphorylation/activation of the kinase is enhanced 2-fold by heparin (0.4 unit/ml) and blocked by phosphatidylserine (0.4 mg/ml). Partial dephosphorylation of the phosphorylated kinase is associated with a time-dependent decrease in the enzyme activity. This autophosphorylation-dependent protein kinase phosphorylates glycogen synthase (Km = 8 microM) at sites 2 and 3, resulting in inactivation of glycogen synthase. The results indicate that this independent kinase may represent a previously undiscovered liver multifunctional protein kinase which can be regulated by reversible phosphorylation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9421-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Characterization of an autophosphorylation-dependent multifunctional protein kinase from liver.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't