In rat liver microsomes, oxytocin competitively inhibited specific [3H]AVP binding with a Ki of 41.4 nM, weaker than AVP at 0.19 nM.
In plain wordsIn lab tests on rat liver membranes, oxytocin blocked vasopressin binding, but much more weakly than vasopressin itself.
- Peptide
- Oxytocin
- Outcome
- Not applicableCompetitive inhibition of [3H]AVP binding (Ki)
- Study
ratn: not reported in source
Rat liver microsomes- Outcome group
- Receptor activity and mechanism · Pharmacology
- Studied dose
- Dose not stated
Measurements
- Ki
- 41.4 nM
- [3H]AVP binding, rat liver microsomes
Source sentences
Competitive inhibition of specific [3H]AVP binding by unlabeled AVP and related peptides showed the following Ki values: AVP, 0.19 nM; LVP, 1.7 nM; oxytocin, 41.4 nM
1 context sentence(design, population, supporting numbers)
A single class of high affinity, low capacity, specific binding sites for [3H]arginine8 vasopressin (AVP) has been characterized in a plasma membrane-enriched microsomal fraction of the rat liver.