title: Antagonist binding reveals two heterogenous B2 bradykinin receptors in rat myometrial membranes.
abstract: In rat myometrial membranes, two bradykinin binding sites with K1 values of 18 pM and 5.6 nM were identified. Three potent bradykinin antagonists were tested for their ability to compete for [3H]bradykinin binding. Two of them, D-Arg[Hyp3,Thi5.8,D-Phe7]bradykinin and [Hyp3,Thi5.8,D-Phe7]bradykinin, also bound to both the high- (KH) and the low-affinity (KL) site whereas [Thi5.8,D-Phe7]bradykinin identified only the low-affinity bradykinin receptor. There is a close correlation between the antagonistic potencies and the KL site affinities.
authors.affiliation: Institute of Biochemistry and Biophysics, Biological Faculty, Friedrich-Schiller-University Jena, F.R.G.
authors.forename: C
authors.initials: C
authors.lastname: Liebmann
authors.forename: M
authors.initials: M
authors.lastname: Schnittler
authors.forename: J M
authors.initials: JM
authors.lastname: Stewart
authors.forename: S
authors.initials: S
authors.lastname: Reissmann
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D005260:Female; D066298:In Vitro Techniques; D007700:Kinetics; D008566:Membranes / Q000378:metabolism / Q000648:ultrastructure; D009215:Myometrium / Q000378:metabolism / Q000648:ultrastructure*; D051381:Rats; D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter / Q000037:antagonists & inhibitors* / Q000145:classification / Q000378:metabolism
chemical_list: D018002:Receptors, Bradykinin; D017981:Receptors, Neurotransmitter