ArticleJournal of peptide science : an official publication of the European Peptide Society2022
Clearance of oxytocin and its potentially enzyme resistant analogues in the OXT-receptor compartment of the potassium depolarized rat myometrium.
Article in Journal of peptide science : an official publication of the European Peptide Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 1 citations in OpenAlex.
- A multiscale PBPK-PD model of oxytocin-induced uterine excitation and contraction.The Journal of physiology · 2026Article
- Clearance of oxytocin and its potentially enzyme resistant analogues in the OXT-receptor compartment of the potassium depolarized rat myometrium.Journal of peptide science : an official publication of the European Peptide Society · 2022Article
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2 authors at 1 institution in 1 country.
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Abstract
The time-response behaviour of a group of oxytocin analogues structurally modified on potential sites of oxytocin splitting by tissue inactivation enzymes ("enzyme probes") was investigated ex vivo on the potassium depolarized rat myometrium (at 30°C) and compared with the data obtained in the in vivo experiments. The modified oil-immersion method by Kalsner and Nickerson was used to record time profiles after cessation of a steady state myometrium contraction triggered by analogues in a high potassium tissue medium. An exchange of the aqueous medium for mineral oil enables to suppress return diffusion of the peptide and to record its irreversible clearance near the corresponding receptor compartment. Response records were analysed by a nonlinear numeric procedure based on combination of steady state and kinetic terms that allows concomitant estimations of affinities from time-response measurements, in the given case for analogues on depolarized myometrium. Potential inactivation-sensitive sites in the oxytocin chain are the Ν-terminal peptide bond Cys
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