Villa-Moruzzi E
Growth. 1985 Winter;49(4):417-25.
The activities of phosphorylase phosphatase and of FA, the kinase that activates phosphatase, were measured in rat skeletal muscle from birth to 200 g body weight. Throughout this period part of phosphatase was always spontaneously active. The activity could be further increased by trypsin, but did not additionally increase when Mn2+ was present. During the first 15-20 days of life most of the phosphatase was cytosolic. Then it decreased in this fraction and more phosphatase was found in glycogen particles, to reach the adult level at about 50 g body weight. Also the activity of the kinase FA was lower for the first 10 days, then it increased attaining the adult level again at about 50 g. These results are compared to those on phosphorylase activity and glycogen level in muscle and on serum insulin during growth.
测定了从出生到体重达200克的大鼠骨骼肌中磷酸化酶磷酸酶以及激活磷酸酶的激酶FA的活性。在整个这一时期，部分磷酸酶一直处于自发活性状态。其活性可被胰蛋白酶进一步提高，但在存在Mn2+时不会额外增加。在出生后的前15 - 20天，大部分磷酸酶存在于胞质溶胶中。然后它在这一部分中减少，而在糖原颗粒中发现更多的磷酸酶，在体重约50克时达到成年水平。激酶FA的活性在最初10天也较低，然后升高，在约50克时再次达到成年水平。将这些结果与生长过程中肌肉中磷酸化酶活性、糖原水平以及血清胰岛素的结果进行了比较。
