Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1992-4-13
pubmed:abstractText
This study reports the localisation of the [32P]IP3 binding site on highly purified membrane fractions prepared using high-voltage free-flow electrophoresis. Binding studies on mixed membranes, carried out at 4 degrees C, revealed a binding site with a Kd = 86 nM and beta max = 5.3 pmol/mg protein. The binding was potently inhibited by heparin. High-voltage free-flow electrophoresis was used to further purify surface and intracellular membranes. The intracellular membranes showed a 5-fold enrichment of binding sites with respect to the parent mixed membranes with the same Kd (80 nM), but the surface membranes showed an absence of binding activity. The results indicate the localisation of the IP3 receptor on highly purified intracellular membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
298
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Localisation of the [32P]IP3 binding site on human platelet intracellular membranes isolated by high-voltage free-flow electrophoresis.
pubmed:affiliation
Platelet Section, Thrombosis Research Institute, Chelsea, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't