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[Kinetic characteristics of creatine kinase and hexokinase from rat skeletal muscles during dietary deficit of vitamin K and administration of pelentane].

Kinetic parameters of rat creatine kinase isozymes at different vitamin K supply and treatment with antivitamin K--pelentan have been determined. MM-isozyme (skeletal muscle) has selective sensitivity to the vitamin K deficit, while BB and MB-isozymes (brain, kidney and heart) have not. The value KM for ATP of MM-isozymes increases, while maximal activity decreases. Pelentan treatment does not lead to the change of MM-creatine kinase affinity to ATP. Soluble hexokinase of skeletal muscle in rats with vitamin K deficiency and treated with pelentan has higher affinity to glucose as compared to normal rat enzyme. It has been supposed that skeletal muscle hexokinase exists in a particular molecular form under vitamin K deficiency.

Animals↗

[The effect of supplying rats with vitamin K and administration of pelentane on Na,K- and spectrin-dependent ATPase in erythrocyte ghosts].

It was found that the activity of spectrin-dependent ATPase of erythrocyte ghosts isolated from rats with alimentary deficiency of vitamin K was significantly increased as compared with control animals, whereas in rats kept on a vicasol-rich diet this parameter was unchanged. In vitamin K-deficient rats the amount of proteins loosely bound to erythrocyte membranes was significantly reduced. At the same time, the activity of the integral enzyme (Na, K-ATPase) did not depend on the vitamin K provision despite the fact that in vitamin K-deficient animals kept on a vicasol-rich diet the enzyme affinity for ouabain was strongly decreased as compared with control. It was suggested that this effect might be due to the changes in the lipid and protein environment of the membrane-bound enzyme. Administration of the antivitamin K, pelentane, did not induce any conspicuous changes in the enzyme activities. It was concluded that antivitamin K does not induce any modification of the properties of erythrocyte-linked enzymes observed under conditions of vitamin K deficiency.

Adenosine Triphosphatases↗

[Metabolic function of isolated liver mitochondria during various conditions of vitamin D and K supply and administration of pelentane].

Alimentary deficiency of vitamin K caused a decrease in the rate of respiration in presence of ADP and in the rate of oxidative phosphorylation in the presence of succinate. Administration of the antivitamin K pelentane, excess of vikasol and deficiency of vitamin D did not affect these parameters. As distinct from controls and rats treated with pelentane, transport of calcium was decreased in presence of all the substrates studied in mitochondria isolated from liver tissue of animals deprived of vitamins K and D as well as of animals treated with vikasol excess. At the same time, accumulation of calcium led to time-dependent inhibition of respiratory chain if NAD-dependent substrates were used. Possible reasons of dissimilarity observed are discussed; the phenomenon found may occur due to exhaustion of the mitochondrial pyridine nucleotides pool. The data obtained suggest that antivitamins K altered only some parameters of body status (prothrombin time) similarly to the alterations observed in alimentary deficiency of vitamin K.

Animals↗

[Status of liver mitochondria and rat tissue creatine kinase during administration of antivitamin K].

It has been shown that 16-18 days administration of antivitamin K (pelentan) leads to two-fold increase of prothrombin time in adult rats but does not influence the soluble brain, renal, heart, muscle and serum creatine kinase activity. No effect on metabolic function of isolated liver mitochondria has been found in contrast to the vitamin K deficient rats. Mitochondria were characterized by high value of respiration control; substance oxidation rates and internal mitochondrial Ca2+ content do not differ in the level from those of control animals. From the obtained results and data published in literature a conclusion can be drawn about only particular similarity (prothrombin time) between the antivitamin K administration and alimentary vitamin K deficit.

Animals↗

[Metabolism of the inhibitor of fibrin self-assembly in rats].

It has been shown that the application of the labelled preparation in physiologically normal white rats and in animals with experimental hyper- and hypothrombinemia leads to the rapid exchange of the peptide self-assembly inhibitor between the blood and extravascular space. The constant level of the inhibitor in the blood is maintained due to continuous supply from tissues and its excretion with the urine. The role and mechanisms of the inhibitor involvement into the maintenance of the liquid state of the blood as a factor limiting the speed of nonenzymatic stage of fibrinogen conversions are suggested.

Animals↗