The present studies were undertaken to better characterize the pharmac
ological properties of oxytocin receptors (OTRs) of the porcine kidney
cell line, LLC-PK1, in their natural membranous environment and after
solubilization. In intact membranes, binding of a selective radioliga
nd was rapid, reversible, saturable, and of high affinity. High-affini
ty agonist binding was reduced by a GTP analogue, suggesting that thes
e OTRs are associated with G-protein(s). After solubilization with the
zwitterionic detergent CHAPSO, OTRs retained their high affinity for
the radioligand and rank order potency for oxytocin analogues, and ago
nist binding remained biphasic and GTP sensitive.