S S Maglysh

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Radiometric assays revealed that thiamine deficiency in rats to whom hydroxythiamine was administered in variable doses, is concomitant with activation of gluconeogenesis from pyruvate in liver tissue. The most probable mechanism of this effect is the cAMP-dependent activation of key enzymes of intracellular glucose synthesis. This process is facilitated by(More)
Phosphopentose stimulation of nucleic acids biosynthesis for 3h after subcutaneous phosphopentose administration in doses of 18 and 27 mg per rat has been stated. Injections of phosphopentoses (ribose-5-phosphate, xylulose-6-phosphate, ribulose-5-phosphate in the ratio of 1.0:0.3:0.3) were followed by a two-fold increase in the rate of [2-14C] orothic acid(More)
B1-hypovitaminosis was simulated in white rats of 150-170 g body mass by means of hydroxythiamin administration at a daily dose of 4, 40 or 100 mg/kg within 10 days. Concentrations of NADP and NADPH, main cofactors of 6-phosphogluconate dehydrogenase, were dissimilarly altered in the animal liver tissue depending on the antimetabolite dose administered.(More)
Thiamine deficiency in rats induced by oxythiamine is accompanied by an increase in the free NADP+/NADPH ratio in liver tissue, which results in multifold stimulation of the metabolite flux in the oxidation branch of the pentose cycle. The increase in the intracellular concentrations of isocitrate and alpha-ketoglutarate with a simultaneous decrease of(More)
Thiamine-deficiency in animals induced by everyday subcutaneous administration of oxythiamine in a dose of 4, 40 and 100 mg/kg of weight for 10 days results in a decrease of the total activity of pyruvate kinase in the liver tissue and does not affect the mentioned index in the kidney and heart tissues. It is shown that as a result of the enzyme(More)
Inhibition of rat liver transketolase under conditions of hydroxythiamin or alimentary B1 avitaminosis was accompanied by an increase in intracellular concentration of 6-phosphogluconate and xylulose-5-phosphate. The alterations in their content was inversely correlated with the transketolase activity. The dehydrogenases involved in the pentose phosphate(More)
Kinetic analysis permitted to determine two sites of hydroxythiamine diphosphate binding in apotransketolase. The Ki values for these sites differed significantly: (7-22) X 10(-9) M and (13.0-19.7) X 10(-8) M. The rate of thiamine diphosphate turnover within holotransketolase in rat liver tissue was studied by the radioisotope method, using [14C]thiamine as(More)
Lactate dehydrogenase M4-isoform in the homogeneous state was isolated from the rat liver by successive application of sulphate-ammonium fractionation, phosphocellulose ion-exchange chromatography with high-affinity elution of 1 mM NADH and subsequent hydroxyl apatite fractionation. The method permits obtaining the preparation amounts of the enzymic protein(More)
Using stepwise protein fractionation by (NH4)2SO4 and ion-exchange chromatography on CM-cellulose, DEAE-cellulose and SP-Sephadex, two isoforms of 6-phosphogluconate dehydrogenase, A and B, from rat liver were obtained. The method developed allows to achieve complete separation of these forms and to obtain preparative amounts of the protein with specific(More)
It was found that the progressive development of vitamin B1 deficiency in rats caused by varying doses of oxythiamine results in a sharp decrease of the free NAD/NADH ratio in the liver after injection of a high dose of the antivitamin. The value of this ratio was calculated from the intracellular concentrations of pyruvate, lactate and Keq for lactate(More)