Linked Life Data

2551069

Source:http://linkedlifedata.com/resource/pubmed/id/2551069

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-10-26
pubmed:abstractText
Binding parameters for the interaction of GTP-gamma-[35S] with isolated platelet plasma membranes have been studied. Analysis of the data by a non-linear curve fitting program indicates that the interaction can be satisfactory described by a model with a single, high affinity binding site (Kd = 0.3 +/- 0.07 microM and Bm = 0.4 +/- 0.2 nmoles of GTP-gamma-S/mg of membrane protein). Binding is selectively inhibited by GDP-beta-S and GMP-PNP (1 microM), but not affected by ATP, CTP, ITP, or UTP, even at mM concentration. Optimal conditions for the interaction were 30 degrees C and pH 8.0. Incubation of the isolated membranes with GTP-gamma-S results in a measurable phospholipase C activity (as detected both by a breakdown of phosphoinositides and an increase of inositide phosphates) which under our experimental conditions is only slightly enhanced by addition of cytosolic proteins. Our results indicate that platelet plasma membranes contain all the necessary elements for signal transduction through the diacylglycerol/inositolphosphates pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
747-56
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Characterization of GTP-gamma-S binding to isolated human platelet plasma membranes and its relationship with the stimulation of a phospholipase C activity.
pubmed:affiliation
U-150 INSERM, UA 334 CNRS, Hôpital Lariboisière, Paris, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't