Results 261 to 270 of about 22,279 (302)
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Enzyme electrode for glucose based on the quinoprotein glucose dehydrogenase

The Analyst, 1985
Glucose dehydrogenase (E.C. 1.1.99.17) has been used to produce an amperometric enzyme electrode for glucose. With phenazine ethosulphate as the electron mediator, a linear response for up to 0.8 mM glucose was obtained with response times of 3–5 min. 2,6-Dichlorophenolindophenol as mediator gave long (> 30 min) response times, but the measurement time
W H, Mullen   +2 more
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Glucose-6-Phosphate Dehydrogenase

1985
Genetic systems have been of interest to human genetics mainly because they exhibit polymorphism in various populations, and therefore seem to be relevant to human evolution, or because they are associated with pathological manifestations. In addition, whereas frequently biological systems are easier to investigate in microorganisms or in experimental ...
L, Luzzatto, G, Battistuzzi
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The quinoprotein dehydrogenases for methanol and glucose

Archives of Biochemistry and Biophysics, 2004
This review summarises our current understanding of two of the main types of quinoprotein dehydrogenase in which pyrroloquinoline quinone (PQQ) is the only prosthetic group. These are the soluble methanol dehydrogenase and the membrane glucose dehydrogenase (mGDH).
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Studies of Amperometric glucose dehydrogenase electrodes for glucose

Analytica Chimica Acta, 1987
Abstract Glucose sensors are constructed by immobilizing glucose dehydrogenase physically or chemically on a carbon or platinum electrode. Soluble coenzyme was used. The usefulness of the electrode is limited by interference from any molecule that can be oxidized at + 450 mV.
G. Palleschi   +3 more
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Radiochemical assay for UDP-glucose dehydrogenase

Analytical Biochemistry, 1972
Abstract A rapid radioisotopic assay was developed for the enzyme UDP-glucose dehydrogenase. The assay is based on formation of UDP-glucuronate- 14 C from UDP-glucose- 14 C. The enzyme product was rapidly separated from unreacted substrate on anion-exchange paper after hydrolysis of the sugar nucleotides to give the sugar acid and neutral sugar.
M D, Davies, D B, Dickinson
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Glucose-6-phosphate dehydrogenase deficiency

Best Practice & Research Clinical Haematology, 2000
Glucose-6-phosphate dehydrogenase (G6PD) is expressed in all tissues, where it catalyses the first step in the pentose phosphate pathway. G6PD deficiency is prevalent throughout tropical and subtropical regions of the world because of the protection it affords during malaria infection.
A, Mehta, P J, Mason, T J, Vulliamy
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Catalytic mechanism of UDP-glucose dehydrogenase

Biochemical Society Transactions, 2019
Abstract UDP-glucose dehydrogenase (UGDH), an oxidoreductase, catalyzes the NAD+-dependent four-electron oxidation of UDP-glucose to UDP-glucuronic acid. The catalytic mechanism of UGDH remains controversial despite extensive investigation and is classified into two types according to whether an aldehyde intermediate is generated in the ...
Jun Chen, Shulin Yang
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Synthesis of glucose dehydrogenase in Bacterium anitratum

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1965
Abstract Cells of Bacterium anitratum have been observed to incorporate radioactive sulphate into the cytochrome-linked glucose dehydrogenase with an initial rate which differs little from the rate of incorporation into the soluble cytoplasmic form of the same enzyme. It does not appear likely therefore that the soluble form is the precursor of the
J G, HAUGE, P A, HALLBERG
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Glucose-6-phosphate dehydrogenase deficiency

The Lancet, 2008
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect, being present in more than 400 million people worldwide. The global distribution of this disorder is remarkably similar to that of malaria, lending support to the so-called malaria protection hypothesis.
M.D. Cappellini, G. Fiorelli
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Placental Glucose Dehydrogenase Polymorphism in Japanese

Human Heredity, 1989
The polymorphism of glucose dehydrogenase (GDH) was investigated in 516 Japanese placentae. The allele frequencies were GDH*1 = 0.510, GDH*2 = 0.488 and GDH*3 = 0.002. GDH*3 appears to increase from Japan via Southeast Asia and India to Europe.
A, Kido, N, Komatsu, Y, Kimura, M, Oya
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