Radioligand analogs of oxytocin bound with high affinity to the same population of sites on LLC-PK1 cell membranes, with mean Kd values of 14 and 0.06 nM.
In plain wordsIn pig kidney cell membranes, two oxytocin-like labels bound tightly to the same oxytocin receptor sites.
- Peptide
- Oxytocin
- Outcome
- Not applicableBinding affinity of oxytocin receptor ligands to LLC-PK1 membranes
- Study
pign: not reported in source
LLC-PK1 and LLC-PK1L pig kidney cell lines- Outcome group
- Receptor activity and mechanism · Kidney and urinary
Measurements
- Kd
- 14 nM
- [3H]-[Thr4,Gly7]OT
- Kd
- 0.06 nM
- 125I-OTA
- Bmax
- 100 fmol/mg membrane protein
- LLC-PK1 membranes
Source sentences
[3H]-[Thr4,Gly7]OT and 125I-OTA bind with high affinity (mean Kd values of 14 and 0.06 nM, respectively) to the same population of sites on LLC-PK1 cell membranes [maximum binding (Bmax) of 100 fmol/mg membrane protein].
1 context sentence(design, population, supporting numbers)
Two selective radioligands for oxytocin receptors, [3H]-[4-threonine,7-glycine]oxytocin [( 3H]-[Thr4,Gly7]OT) and 125I-[1-(beta-mercapto-beta,beta-cyclopentamethylenepropionic acid), 2-(O-methyl)tyrosine, 4-threonine, 8-ornithine, 9-tyrosine amide]-oxytocin (125I-OTA), were used to characterize oxyt…
In this study, Oxytocin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Oxytocin.