form
lyophilized powder
specific activity
2-10 units/mg protein
composition
Protein, ~80%
foreign activity
Hexokinase and glucose-6-phosphate dehydrogenase <0.3%
storage temp.
−20°C
Physical form
Lyophilized powder containing Tris buffer
Analysis Note
Protein determined by biuret
Other Notes
One unit will oxidize 1.0 μmole of 6-phospho-D-gluconate to D-ribulose 5-phosphate and CO2 per min at pH 7.4 at 37 °C in the presence of NADP+.
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Weiwei He et al.
BMC structural biology, 7, 38-38 (2007-06-16)
As the third enzyme of the pentose phosphate pathway, 6-phosphogluconate dehydrogenase (6PGDH) is the main generator of cellular NADPH. Both thioredoxin reductase and glutathione reductase require NADPH as the electron donor to reduce oxidized thioredoxin or glutathione (GSSG). Since thioredoxin
Y Katsumata et al.
Journal of forensic sciences, 27(1), 192-195 (1982-01-01)
Attempts were made to detect phenotypes of the enzymes phosphoglucomutase (PGM) and phosphogluconate dehydrogenase (PGD) in human skin and adipose tissues. Both enzymes could be typed using approximately 3 mg wet weight of tissue. Phenotypes could be distinguished after up
Hülya Demir et al.
Preparative biochemistry & biotechnology, 33(1), 39-52 (2003-04-16)
In this study, 6-phosphogluconate dehydrogenase (E.C.1.1.44; 6PGD) was purified from parsley (Petroselinum hortense) leaves, and analysis of the kinetic behavior and some properties of the enzyme were investigated. The purification consisted of three steps that are preparation of homogenate ammonium
M Zelewski et al.
Biochemistry international, 19(5), 1057-1065 (1989-11-01)
The effect of starvation-refeeding transitions on the activity of malic enzyme and hexosemonophosphate shunt dehydrogenases in lipogenic and non-lipogenic tissues from rats was investigated. Starvation of the rats caused a decrease of malic enzyme activity in the liver, white and
L Minchiotti et al.
Biochimica et biophysica acta, 657(1), 232-242 (1981-01-15)
6-Phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP+ 2-oxidoreductase(decarboxylating), EC 1.1.1.44) from Candida utilis is inhibited by reaction with pyridoxal 5'-phosphate. The aldehydic group of this compound forms a Schiff base with the epsilon-amino group of a lysine residue: reduction of this enamine with
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