Results 131 to 140 of about 8,459 (174)
Some of the next articles are maybe not open access.
Kinetic Studies of Mouse Brain Transketolase
Journal of Neurochemistry, 1982Abstract: The activity of transketolase in mouse brain was 5.7 nmol/min/mg protein measured by an enzyme‐coupled spectrophotometric assay. The apparent Km for ribose‐5‐phosphate was 330 μM, for d‐xylulose‐5‐phosphate was 120 μM, and for thiamine pyrophosphate was 7 μM.
J P, Blass +3 more
openaire +2 more sources
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
openaire +2 more sources
The Catalytic Mechanism of Human Transketolase
ChemPhysChem, 2019AbstractWe have computationally determined the catalytic mechanism of human transketolase (hTK) using a cluster model approach and density functional theory calculations. We were able to determine all the relevant structures, bringing solid evidences to the proposed experimental mechanism, and to add important detail to the structure of the transition ...
Prejano M. +5 more
openaire +2 more sources
Bioscience, Biotechnology, and Biochemistry, 1993
Given the importance of transketolase, TK (EC 2.2.1.1) for both pharmacological studies and synthetic purposes, the need for a simple and inexpensive assay is patent. We describe here a simple and inexpensive TK assay using the unphosphorylated ketoses L-erythrulose, 4-deoxy-L-erythrulose, and 4-deoxy-D,L-erythrulose as donor substrates instead of D ...
Laurence Hecquet +2 more
openaire +1 more source
Given the importance of transketolase, TK (EC 2.2.1.1) for both pharmacological studies and synthetic purposes, the need for a simple and inexpensive assay is patent. We describe here a simple and inexpensive TK assay using the unphosphorylated ketoses L-erythrulose, 4-deoxy-L-erythrulose, and 4-deoxy-D,L-erythrulose as donor substrates instead of D ...
Laurence Hecquet +2 more
openaire +1 more source
Functional Flexibility of the Transketolase Molecule
Biochemistry (Moscow), 2001Transketolase is the simplest representative of the thiamine diphosphate-dependent enzymes. It was the first of these enzymes for which X-ray analysis was performed. Based on the data of X-ray studies and using the mutagenesis technique, the nature of functional groups of the enzyme involved in the interaction with substrates and cofactors and in the ...
openaire +2 more sources
Erythrocyte Transketolase Activity
The American Journal of Clinical Nutrition, 1970Y H, Chong, G S, Ho
openaire +2 more sources
Erythrocyte Transketolase Inhibition, Neuropathy and Uremia
New England Journal of Medicine, 1971The first clinically successful treatment of renal failure with the artificial kidney by W. J. Kolff in 1943 must be regarded as an empirical triumph. Although several normal solutes had been identified in abnormally high concentration in the blood of uremic patients, there was no information about whether reducing their concentrations would restore ...
openaire +2 more sources
Clinical Application of Blood Transketolase Determinations
New England Journal of Medicine, 1962A NUMBER of biochemical tests have been designed and employed to aid in the overall assessment of the nutritional state of patients thought to be suffering from a vitamin deprivation. Many of these tests are cumbersome and poorly reproducible, and some lack specificity.
openaire +2 more sources

