Abstract:
:The present studies were undertaken to better characterize the pharmacological 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 radioligand was rapid, reversible, saturable, and of high affinity. High-affinity agonist binding was reduced by a GTP analogue, suggesting that these 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 agonist binding remained biphasic and GTP sensitive.
journal_name
Peptidesjournal_title
Peptidesauthors
Flanagan-Cato LM,Moga CN,Fluharty SJdoi
10.1016/0196-9781(95)02121-3subject
Has Abstractpub_date
1996-01-01 00:00:00pages
251-6issue
2eissn
0196-9781issn
1873-5169pii
0196-9781(95)02121-3journal_volume
17pub_type
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