Results 211 to 220 of about 174,209 (261)
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Glucose-6-Phosphate Dehydrogenase Velletri
Acta Haematologica, 2009A new variant of red cell glucose-6-phosphate dehydrogenase (G6PD) has been found in a Caucasian man with congenital non-spherocytic haemolytic anaemia. This variant has reduced activity, increased thermolability, increased Michaelis constants for glucose-6-phosphate and NADP, slightly increased electrophoretic mobility, and a biphasic pH-activity ...
F, Mandelli +5 more
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Glucose-6-phosphate dehydrogenase deficiency
The Lancet, 2008Glucose-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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Glucose-6-Phosphate Dehydrogenase
1985Genetic 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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Glucose 6-phosphate dehydrogenase and the kidney
Current Opinion in Nephrology and Hypertension, 2017Glucose 6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway. G6PD is the main source of the essential cellular reductant, NADPH. The purpose of this review is to describe the biochemistry of G6PD and NADPH, cellular factors that regulate G6PD, normal physiologic roles of G6PD, and the pathogenic role altered ...
Netanya Y, Spencer, Robert C, Stanton
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Variants of Glucose 6-Phosphate Dehydrogenase
Annals of Internal Medicine, 1968Excerpt Glucose 6-phosphate dehydrogenase (G6PD) is the enzyme that catalyzes the first step in the pentose phosphate shunt.
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Glucose-6-phosphate dehydrogenase deficiency
Baillière's Clinical Haematology, 1992Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzymopathy. Because its gene locus is on the X-chromosome it is more common in males than females in all populations. Prevalence rates vary from 62% among Kurdish Jews to the very low rates (0.1% or less in Japan, for example), which are compatible with sporadic cases arising
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Inhibition of glucose-6-phosphate dehydrogenase by steroids
Journal of Steroid Biochemistry, 1971Abstract By incubation of purified human placental glucose-6-phosphate dehydrogenase (G-6-PDH) with DHA. its conjugates or other derivatives, it could be demonstrated that DHA sulfate, phosphate and glucuronoside do not inhibit this enzyme. Conversely, DHA sulfatide proved to be extremely active in the enzyme inhibition test, whereas lipophite DHA ...
P, Benes, G W, Oertel
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Muscle glucose-6-phosphate dehydrogenase deficiency
Journal of Neurology, 1989Muscle glucose-6-phosphate dehydrogenase (G6PD) deficiency is described in four clinically heterogeneous patients: an athlete who developed myoglobinuria after physical exercise; a 7-year-old, mildly mentally retarded boy, who had episodes of dark urine and high creatine kinase; and two brothers of Sardinian origin, the elder showing moderate exercise ...
N, Bresolin +9 more
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Favism and Glucose-6-Phosphate Dehydrogenase Deficiency
New England Journal of Medicine, 2018Favism and Glucose-6-Phosphate Dehydrogenase Deficiency When persons with G6PD deficiency eat fava beans, acute hemolytic anemia may develop. It is caused by the generation of free radicals from the metabolism of glucosides in the beans. The free radicals damage red cells, resulting in intravascular and extravascular lysis.
Michael, Steiner +2 more
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Athens Variant of Glucose-6-Phosphate Dehydrogenase
Science, 1967A variant of glucose-6-phosphate dehydrogenase (G6PD), characterized by slower than normal electrophoretic migration and associated with mild deficiency of G6PD in the red cells, was detected in two unrelated Greek males. Electrophoretic, chromatographic, and enzymologic study indicated that the new mutant is structurally different from normal G6PD (B+)
G, Stamatoyannopoulos +3 more
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