enzyme is stimulated in presence of 3 mg and 5 mg of Cd on the first day of experiment in gill, liver and kidney tissues. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PD enzyme activity levels are stimulated by approximately 60% in gills
in patients with type 1 diabetes G6PDH activity does not differ from control group, but enzyme activity is sharply decreased in pregnant women with type 2 diabetes and gestational diabetes
moderate overexpression of the enzyme (G6PD) can protect beta-cells from age-associated oxidative stress thus reducing the risk of developing type 2 diabetes. The animal show an improved glucose tolerance and insulin sensitivity when compared to old age-matched wild type ones
extralesional and wild-type, the lesions show a 20fold higher, and extralesional parenchyma a 2fold higher, virtual flux at physiological substrate concentrations compared to normal parenchyma
negative correlation between locomotion of rats in the open field and activity of G-6-PDH in the sensorimotor cortex, especially in efferent layer V neurons and neurons of the caudate nucleus and nucleus accumbens, which attests to different capacity of the brain in Wistar rats with high and low open-field locomotion to regeneration of phosphopyridine nucleotides (NADP(+)) and production of pentoses via the pentose phosphate shunt. No correlation between enzyme activity in the hippocampus and locomotion
KlZWF1 is constitutively expressed. Its deletion leads to increased sensitivity to hydrogen peroxide on glucose. The Klzwf1DELTA strain has a reduced biomass yield on fermentative carbon sources as well as on lactate and glycerol
enzyme activity of G6PD enzyme is significantly stimulated after three days in liver and kidney tissues at a dose of 1 mg/l Cdand is stimulated on the first day of experiment in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 67% in kidney
enzyme activity of G6PD enzyme is significantly stimulated after three days in liver and kidney tissues at a dose of 1 mg/l Cd and is stimulated on the first day of experiment in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 68% in liver
glucose-6-phosphate dehydrogenase plays a pivotal role in nitric oxide-involved defense against oxidative stress under salt stress in red kidney bean roots
the enzyme is detected throughout the growth phase. The substantial increase in G6PDH-1 observed at stationary phase or as the results of external oxidative stress indicates that this enzyme is inducible under stressful environmental conditions
G6PD activity is higher in healthy small rather than large follicles, with similar glutathione concentration in both cases. Activity of G6PD decreases in atretic small follicles, but not in large ones. Specific activity of G6PD and glutathione concentrations in the atretic follicular fluid are lower than those in granulosa cells (10- and 5times respectively) in all kind of follicles. The higher G6PD activity in the small follicles may be related to granulosa cell proliferation, follicular growth, and a lower sensitivity to oxidative stress when compared with large follicles. Lower G6PD activity in large follicles indicating a higher susceptibility to oxidative stress associates to apoptosis progression in follicle atresia
different patterns of glucose-6-phosphate dehydrogenase activities are observed among strains Tulahuen S and Y along the growth curve and when cells are challenged with H2O2