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Biomedical subjects

G L Antoniak

Publications and source records attributed to G L Antoniak.

6 recordsLinked to original sources
PubMedDate not supplied

[The effect of hypoxic hypoxia on the activity of glycolysis enzymes in rat erythrocytes].

The oxygen-binding properties of hemoglobin, concentration of 2,3-diphosphoglycerate, activity of carbohydrate metabolism enzymes and kinetics of rat erythrocyte hemolysis have been studied at high altitudes. The hemoglobin affinity to oxygen, glycolysis enzyme activity and erythrocyte membrane resistance are established to increase at the initial period of adaptation. The activation of the pentose-phosphate pathway of the glucose, transformation and inhibition of the glycolytic process in these cells are observed on the 10th day.

2,3-Diphosphoglycerate↗
PubMedDate not supplied

[Insulin-degrading neutral protease from plasma membranes of rat liver cells and erythrocytes].

Insulin-degrading neutral proteinase with molecular weight of 70 kDa was partly purified from the rat liver and erythrocyte plasma membranes. Incubation of membranes with [gamma-32P]ATP resulted in the enzyme phosphorylation. Intensity of this process greatly increased in the presence of insulin (100 microU/ml), and correlated with the elevation of the insulin-degrading activity in proteinase. Ca2+, Mn2+, dithiothreitol, cysteine were shown to have a stimulatory effect on insulin degradation; p-chloromercuribenzoate significantly repressed this process. Phenylmethylsulphonyl fluoride and soybean trypsin inhibitor did not affect the activity of the proteinase. It was concluded that the investigated enzyme was a calpain and may participate in the mechanism of insulin action.

Animals↗
PubMedDate not supplied

[Oxygen-transport function and carbohydrate metabolism in rat erythrocytes during hypoxic hypoxia and treatment with insulin].

Hemoglobin affinity to oxygen, enzyme activity and metabolite concentration of carbohydrate metabolism were determined in erythrocytes of rats which were administered insulin solution. A valid decrease of the hemoglobin value P50 (pressure of hemoglobin half-saturation with oxygen), as well as a decrease of the enzyme activity of 2,3-diphosphoglycerate shunt and increase of the activity of regulatory glycolysis enzymes--hexokinase and pyruvate kinase in erythrocytes with multiple introduction of hormones to animals have been established. Such changes in rat erythrocytes were registered with the simultaneous effect of insulin and hypoxic hypoxia evoked by the "lift" of rats in the altitude chamber to the conditional altitude of 9000 m. It is found out that preliminary injection of insulin considerably increases survivability of rats under hypoxic hypoxia at great altitudes.

Animals↗
PubMedDate not supplied

[Effect of thyroxine on the hemoglobin affinity to oxygen and 2,3-diphosphoglycerate level in rat erythrocytes].

Affinity of hemoglobin to oxygen was studied in rat erythrocytes under conditions of intraperitoneal administration of thyroxin in a dose of 0.4 mg per 100 g of animal weight each 24 h for five days. A significant right shift of the oxyhemoglobin dissociation curve is observed only on the 6th day simultaneously with the increase of the 2,3-diphosphoglycerate level in erythrocytes in the period under study. The results obtained from the study of the thyroxin effect on the respiratory function of hemoglobin permit recommending it as an antihypoxant.

2,3-Diphosphoglycerate↗
PubMedDate not supplied

[Insulin binding by erythroid cells of swines].

Insulin binding by erythroid cells of newborn and 1-, 10-, 30-days pigs was investigated. The process intensity in piglets was found to decline in the period from birth to 30 days of life. The obtained changes were determined by the reduced receptors number in high affinity site in early postnatal ontogenesis as well as by decrease of receptor affinity constants in 30-days animals. During investigated period the level of insulin binding by erythrocytes was conditioned by hormone binding ability of "young" erythroid cells, which was found to be high in newborn and decreased considerably in 10-30 days pigs. It was established that postnatal decrease of insulin binding by erythrocytes occurred simultaneously with sharp increase of insulin concentration in animal during the 10-days period after birth. So, it is supposed that insulin may be involved in regulation of its own receptor number in erythrocytes.

Aging↗