Linked Life Data

2542758

Source:http://linkedlifedata.com/resource/pubmed/id/2542758

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-6-26
pubmed:abstractText
The binding of gastrin-releasing peptide (GRP) to rat brain membranes was characterized. GRP binds specifically to a high affinity site in rat brain membranes, with a Kd equal to 2 nM and Bmax equal to 5 pmol/g wet weight of tissue. The specific binding is saturable, reversible, and dependent on tissue concentration, time of incubation, and the pH of the buffer. Hippocampus, cortex, and striatum contained the highest concentration of high affinity binding sites and the thalamus the lowest. The affinities of GRP, bombesin, and their analogues for the GRP receptor were determined. GRP(14-27) and [Tyr4]bombesin had the greatest affinity, whereas GRP(1-16), which lacks the COOH terminal region, had no affinity for the receptor. GRP, bombesin, and analogues stimulate the breakdown of phosphatidylinositol in rat brain hippocampal minces and potencies correspond to their affinities for the GRP receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
689-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Gastrin-releasing peptide receptor in rat brain membranes: specific binding and stimulation of phosphoinositide breakdown.
pubmed:affiliation
Pharmacology Division, Wellcome Research Laboratories, Research Triangle Park, North Carolina 27709.
pubmed:publicationType
Journal Article, In Vitro