Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1990-9-11
pubmed:abstractText
The receptor for the neuropeptide gastrin-releasing peptide, the mammalian homologue of bombesin, was solubilized from rat brain and Swiss 3T3 cells by using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS) and the cholesteryl hemisuccinate ester (CHS). Only the combination of the detergent CHAPS and the cholesteryl ester CHS in a glycerol-containing buffer satisfactorily preserved the binding activity upon solubilization. Specific binding activity was only solubilized from cell lines and tissue preparations known to express the GRP receptor. The dissociation constant (Kd) for the receptor solubilized from rat brain and Swiss 3T3 cells was 0.6 nM, similar to the value of 0.8 nM calculated for the membrane-bound receptor. Binding was saturable and reached equilibrium after approximately 2 h at 4 degrees C. The identity of the solubilized receptor with the membrane-bound one was further confirmed by the concordance of the relative binding affinities of various established bombesin analogues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5153-60
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Solubilization of the receptor for the neuropeptide gastrin-releasing peptide (bombesin) with functional ligand binding properties.
pubmed:affiliation
Rorer Biotechnology, Inc., King of Prussia, Pennsylvania 19406.
pubmed:publicationType
Journal Article