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L S Mil'man

Publications and source records attributed to L S Mil'man.

50 records · Page 3Linked to original sources

[Changes in the activity of enzymes of glycogen metabolism in oocytes and embryos of teleosts].

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.

Animals↗

[The rate of gluconeogenesis and the activity of its key enzymes in the kidneys of the developing chick embryo].

The rate of glucose formation from lactate was studied in tubules isolated from the kidneys of chick embryos of different age and for one- and two-day-old chickens. Changes in the activity of the key enzymes of gluconeogenesis have also been followed in the chick embryo kidneys. The rate of gluconeogenesis markedly increased after hatching. Changes in the rate of gluconeogenesis during embryogenesis are correlated with those in the activity of key enzymes of this process: phospho(enol) pyruvate carboxykinase, fructose-1,6-bisphosphatase, and glucose-6-phosphatase. Glucose-6-phosphatase was shown to be polyfunctional in the kidneys of chick embryos and chickens: in addition to hydrolysis of glucose-6-phosphate with formation of glucose, the enzyme is capable of phosphorylating glucose with the help of phosphate donors, carbamyl-phosphate and pyrophosphate.

Animals↗