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[Physico-chemical properties of uterine smooth muscle actomyosin]
The actomyosin complex of human myometrium has a low Ca-activated ATPase activity (0.007-0.012 mu mole H+ per 1 mg protein for 1 min), small degree and rate of superprecipitation. Transition to the state of pregnancy is accompanied by considerable changes in the physicochemical properties of the myometrium actomyosin. ATPase activity is 5-10 times as high and the rate of superprecipitation rises, particularly after the increase in the calcium concentration. The content of nucleic acid in the actomyosin complex decreases and D280/D260=1.1. The intensity of the actomyosin fluorescence at the pregnant state is more than twice as high.
The actomyosin complex of human myometrium has a low Ca-activated ATPase activity (0.007-0.012 mu mole H+ per 1 mg protein for 1 min), small degree and rate of superprecipitation. Transition to the state of pregnancy is accompanied by considerable changes in the physicochemical properties of the myometrium actomyosin. ATPase activity is 5-10 times as high and the rate of superprecipitation rises, particularly after the increase in the calcium concentration. The content of nucleic acid in the actomyosin complex decreases and D280/D260=1.1. The intensity of the actomyosin fluorescence at the pregnant state is more than twice as high.