[ATPase activity and fluorescence of myometrial actomyosin in experimental uterine inertia].

A comparative study was performed for actomyosin complexes of the female rabbit myometrium in the state of labour (actomyosin of the control) and secondary uterine inertia (actomyosin of the model). Under the secondary uterine inertia the activity of actomyosin Ca2+- and Mg2+-ATPase decreases. When pH of the medium changes, ATPase of control actomyosin has two peaks of the activity: at rH 6.0 and pH 9.0, that of the model at pH 6.0. Actomyosin of the model and control differs by a degree and rate of superprecipitation, thermal stability and structure. It is supposed that the structural changes in actomyosin under the secondary uterine inertia occur due to accumulation of the metabolism products, the level of which with this pathology is beyond the limits of the adaptation potentialities of the organism.