Iurovitskiĭ I U, Mil'man L S
Biokhimiia. 1975 Sep-Oct;40(5):962-8.
An acceleration of the rate of glycogenolysis after the onset of embryo-genesis of the loach (Misgurnus fossilis L.) is not due either to the activation of phosphorylase, nor to the increase of its intracellular activity. The activity of debranching enzyme-amylo-1,6-glucosidase and oligo-1,4 leads to 1,4-glucantransferase are increased, which indicated possible participation of these enzymes in the control of glycogenolysis. The activity of glycogen synthetase reached its maximum before the oocyte maturation and then it gradually decreased. The activity of "branching" enzyme alpha-1,4-glucan: alpha-1,4-glucan 6-glycosyltransferase sharply increased after the beginning of decreasing in the activity of glycogen synthetase. Most of the activity of phosphorylase and debranching enzymes is not bound with the granular glycogen.
泥鳅（Misgurnus fossilis L.）胚胎发生开始后糖原分解速率的加快既不是由于磷酸化酶的激活，也不是由于其细胞内活性的增加。脱支酶 - 淀粉 -1,6-葡萄糖苷酶和寡聚 -1,4 转1,4-葡聚糖转移酶的活性增加，这表明这些酶可能参与糖原分解的调控。糖原合成酶的活性在卵母细胞成熟前达到最大值，然后逐渐下降。糖原合成酶活性开始下降后，“分支”酶α-1,4-葡聚糖：α-1,4-葡聚糖6-糖基转移酶的活性急剧增加。磷酸化酶和脱支酶的大部分活性与颗粒状糖原无关。
