【摘要】 在中国对虾肌动球蛋白（Ａｏｔｏｍｙｏｓｉｎ）经冷冻变性和热变性后，对Ｃａ２＋－ＡＴＰａｓｅ、Ｍｇ２＋－ＡＴＰａｓｅ活性及蛋白质溶解度进行了研究。冷冻变性之后，肌动球蛋白Ｃａ２＋－ＡＴＰａｓｅ活性呈逐渐下降趋势，一般贮藏温度越低，活性降低越快。热变性之后，肌动球蛋白Ｃａ２＋或Ｍｇ２＋－ＡＴＰａｓｅ活性都随温度升高而下降，但肌动球蛋白Ｃａ２＋或Ｍｇ２＋－ＡＴＰａｓｅ活性在３５℃有一急剧下降的拐点，并分别在４５℃、４０℃附近低到０。由于蛋白质的变性，其溶解度也降低更多还原

【Abstract】 The Ca 2+ or Mg 2+ -ATPase activity and solubility of actomyosin(AM) from Penaeus Chinensis due to freeze and thermal denaturation were studied. After freezing denaturation, the Ca 2+ -ATPase activities of AM decreased gradually. In general, the activities decreased at a faster rate with decreasing temperature. After thermal denaturation, the Ca 2+ or Mg 2+ -ATPase of AM have a turn point at 35℃, and 0 at 45℃ and 40℃, respectively. With the increase of temperature, the solubility of the protein also decreased gradually because of denaturation and aggregation of the protein. All these changes may be due to the protein character of AM of prawns muscle.更多还原