The nature of receptor binding of oxytocin in myometrial tissue.

The dissociation course of the hormone receptor complexes of rat myometrial oxytocin receptors was studied. The dissociation course was biphasic with a major component displaying an almost irreversible binding character (time constant 0.003 min-1). This irreversibility was independent of hormonal status of the myometrium as well as the type of divalent cation present in the medium, and was not caused by endocytosis of the receptor. However, as addition of EDTA caused an immediate dissociation of all receptor binding, the irreversibility must be of a non-covalent character. It is suggested that new analysis methods for receptor kinetics including the possibility of partly irreversible binding mechanisms should be considered.