Linked Life Data

10384965

Source:http://linkedlifedata.com/resource/pubmed/id/10384965

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-7-20
pubmed:abstractText
Glycosylphosphatidylinositol-specific phospholipase D (GPI-PLD) was phosphorylated in vitro by cAMP-dependent protein kinase (PKA) and by tyrosine kinase. Phosphorylation by PKA occurred in the 110 kDa native form of GPI-PLD as well as in multiple proteolytic degradation products and caused a significant decrease in enzyme activity. Dephosphorylation by treatment with alkaline phosphatase completely restored GPI-PLD activity. In addition, incubation of GPI-PLD with trypsin, which results in the generation of distinct peptide fragments, resulted in complete dephosphorylation of radiolabeled GPI-PLD. The site of phosphorylation by PKA was assigned to Thr-286. Tyrosine phosphorylation was only observed in a proteolytically processed fragment of GPI-PLD but not in the 110 kDa native form and had no effect on GPI-PLD activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
380
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
In vitro phosphorylation of purified glycosylphosphatidylinositol-specific phospholipase D.
pubmed:affiliation
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't