Results 161 to 170 of about 10,904 (208)
British Journal of Cancer, 2006 Tumours ferment glucose to lactate even in the presence of oxygen (aerobic glycolysis; Warburg effect). The pentose phosphate pathway (PPP) allows glucose conversion to ribose for nucleic acid synthesis and glucose degradation to lactate.
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Substrate inhibition of transketolase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2016We studied the influence of the acceptor substrate of transketolase on the activity of the enzyme in the presence of reductants. Ribose-5-phosphate in the presence of cyanoborohydride decreased the transketolase catalytic activity. The inhibition is caused by the loss of catalytic function of the coenzyme-thiamine diphosphate. Similar inhibitory effect
Olga N, Solovjeva +2 more
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The affinity chromatography of transketolase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978A number of possible affinity adsorbents for transketolase (sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphateglycolaldehydetransferase, EC 2.2.1.1) were prepared. The behaviour of the enzyme from Candida utilis and from Baker's yeast on columns of these and of Blue Sepharose CL-6B was examined, together with the behaviour of the contaminating ...
T, Wood, S, Fletcher
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The electrophoresis and detection of transketolase
Analytical Biochemistry, 1981Abstract After electrophoresis impure transketolase preparations stained readily with an activity stain based on a published method, but pure preparations gave no reaction. The bands first obtained were due to the presence of (i) a transketolase- d -glyceraldehyde-3-phosphate dehydrogenase complex, (ii) alcohol dehydrogenases, and (iii) a zone of ...
T, Wood, C C, Muzariri
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Topics in Catalysis, 2013
Transketolase is an enzyme catalysing asymmetric C–C bond formation which is of great interest for many syntheses of biologically active compounds. Enzymatic couplings present many advantages (mild reaction conditions notably), nonetheless their utilisation on an industrial scale is often limited by restricting factors as their activity, substrate ...
Adeline Ranoux, Ulf Hanefeld
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Transketolase is an enzyme catalysing asymmetric C–C bond formation which is of great interest for many syntheses of biologically active compounds. Enzymatic couplings present many advantages (mild reaction conditions notably), nonetheless their utilisation on an industrial scale is often limited by restricting factors as their activity, substrate ...
Adeline Ranoux, Ulf Hanefeld
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Inhibition of transketolase by hexacyanoferrate(III)
Biochemistry (Moscow), 2010The effect of hexacyanoferrate(III) on the catalytic activity of transketolase has been studied. This oxidant inactivates only one of two active sites of the enzyme, the one with a higher affinity to the coenzyme (thiamine diphosphate). The second active site does not lose its catalytic activity.
V A, Yurshev +3 more
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Inhibition of transketolase by analogues of the coenzyme
Biochemical and Biophysical Research Communications, 1971Abstract The effect of thiamine, thiamine monophosphate, pyrophosphate and thiazole pyrophosphate on the enzymatic activity of transketolase has been studied. All these compounds have been proved to inhibit the enzyme by competing with the coenzyme (thiamine pyrophosphate) for apotransketolase.
G A, Kochetov +2 more
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Erythrocyte transketolase activity in uremia
Clinica Chimica Acta, 1980We performed a study concerning the activity of erythrocyte transketolase and thiamine metabolism in 73 uremic patients with or without neuropathy and 67 normal control subjects. Although the total vitamin B1 level in whole blood was high in the uremic patients, the transketolase activity in the hemolysate and the thiamine pyrophosphate effect on it ...
M, Kuriyama +4 more
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Analysis of Blood Transketolase Activity
American Journal of Clinical Pathology, 1971The determination of blood transketolase (TK) activity is based on the incubation of lysed erythrocytes with and without added thiamine pyrophosphate (TPP). The increased TK activity resulting from the addition of TPP coenzyme is inversely related to thiamine depletion.
M F, Massod, S L, McGuire, K R, Werner
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Isolation and properties of human transketolase
Biochemistry (Moscow), 2010Recombinant human (His)(6)-transketolase (hTK) was obtained in preparative amounts by heterologous expression of the gene encoding human transketolase in Escherichia coli cells. The enzyme, isolated in the form of a holoenzyme, was homogeneous by SDS-PAGE; a method for obtaining the apoenzyme was also developed.
L E, Meshalkina +4 more
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