Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-8-13
pubmed:abstractText
Monoclonal antibodies prepared against clathrin-coated vesicles cargo molecules were screened for their ability to precipitate the mAChR binding activity present in a light-density smooth membrane fraction from bovine brain called peak I. Only monoclonal antibody 10C7 was able to selectively sediment 38% (+/- 4.2) of the mAChR binding activity of peak I. Analysis by competition experiments of the supernatant obtained after the immunoprecipitation step reveals that neither the ratio of high/low affinity sites, nor the affinity ratio KH/KL was significantly altered for either of the muscarinic antagonists. The data implies that the bovine brain smooth-membrane compartment(s) expressing the mAb 10C7 antigen is also enriched in M1 and M2 mAChR.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-94
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Immunoprecipitation of bovine brain membranes enriched in M1 and M2 muscarinic receptors with monoclonal antibody 10C7.
pubmed:affiliation
Department of Pharmacology, Universidad Central del Caribe School of Medicine, Cayey, PR 00634.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.