[3H]Bradykinin receptor binding in mammalian tissue membranes.
AUTOR(ES)
Innis, R B
RESUMO
[3H]Bradykinin binds to membranes from a variety of mammalian tissues in a saturable fashion with a dissociation constant of about 5 nM. Highest levels of binding are detected in guinea pig ileum, colon, and duodenum and in the oestrus rat uterus. The relative potencies of bradykinin derivatives in competing for these binding sites in guinea pig ileum membranes correlate with their contractile potencies in the ileum better than with contractile effects in the uterus. Thus, receptor recognition sites may differ in ileum and uterus. Monovalent and divalent cations at physiological concentrations reduce [3H]bradykinin binding. Of the monovalent cations, medium lowers binding 50% at about 80 mM. Among the divalent cations, calcium lowers binding about 50% at 5 mM, suggesting a link to the calcium conductance channel.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319403Documentos Relacionados
- Binding of [3H]forskolin to rat brain membranes.
- Solubilization and characterization of high-affinity [3H]serotonin binding sites from bovine cortical membranes.
- Sigma opiates and certain antipsychotic drugs mutually inhibit (+)-[3H] SKF 10,047 and [3H]haloperidol binding in guinea pig brain membranes.
- Characterization of beta-endorphin binding protein (receptor) from rat brain membranes.
- The Binding of [3H]Thyrotropin and an 3H-Labeled Exophthalmogenic Factor by Plasma Membranes of Retro-orbital Tissue
