Linked Life Data

2500363

Source:http://linkedlifedata.com/resource/pubmed/id/2500363

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-7-28
pubmed:abstractText
Antibodies generated to a synthetic decapeptide, RMHLRQYELL, representing the carboxyl-terminus of Gs-alpha have been characterized in immunoblots and functional studies. This antibody, designated RM, reacts exclusively with a doublet of proteins of 52 and 45 kDa in immunoblots of bovine brain and wild-type S49 murine lymphoma cell membranes. No such reactivity is seen in membranes from cyc- S49 cells, which lack Gs. RM blocks receptor-mediated activation of Gs and adenylyl cyclase in membranes from wild-type S49 cells. RM could also immunoprecipitate adenylyl cyclase activity in detergent extracts from GTP[gamma]S- or fluoride-preactivated bovine brain membranes; thus binding of alpha s to effector and carboxyl-terminal antibody was mutually compatible. Such experiments provide an approach for the elucidation of functionally relevant interactions of G-proteins with receptors and effectors in the membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
249
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-94
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Receptor and effector interactions of Gs. Functional studies with antibodies to the alpha s carboxyl-terminal decapeptide.
pubmed:affiliation
Molecular Pathophysiology Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892.
pubmed:publicationType
Journal Article