Changes in the activity of enzymes of glycogen metabolism in oocytes and embryos of teleosts
Iurovitskiĭ, I.U.; Mil'man, L.S.
Biokhimiia 40(5): 962-968
1975
ISSN/ISBN: 0320-9725 PMID: 813783 Document Number: 91534
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.