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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-602-6
MDL number:
Specific activity:
200-400 units/mg protein (modified Warburg-Christian)
type
Type XV
Quality Level
form
lyophilized powder
specific activity
200-400 units/mg protein (modified Warburg-Christian)
mol wt
128 kDa
purified by
crystallization
application(s)
diagnostic assay manufacturing
shipped in
dry ice
storage temp.
−20°C
General description
Glucose 6-phosphate dehydrogenase (G-6-P-DH) is a key regulatory enzyme in the first step of the pentose phosphate pathway. G-6-P-DH is a glycoprotein with a molecular mass of 128 kDa (gel filtration).
Application
Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm.
Biochem/physiol Actions
Glucose-6-phosphate dehydrogenase catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway<<<17>>>.
Glucose-6-phosphate dehydrogenase catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway.
Physical form
Lyophilized and essentially sulfate-free; contains approx. 20% sodium citrate based on dry weight
Preparation Note
Prepared from G7877
Other Notes
One unit will oxidize 1.0 μmole of D-glucose 6-phosphate to 6-phospho-D-gluconate per min in the presence of NADP at pH 7.4 at 25 °C.
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Protocols
To measure glucose-6-phosphate dehydrogenase activity, beta-nicotinamide adenine dinucleotide phosphate is used in a spectrophotometric rate determination assay at 340 nm.
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Instructions
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D C Doehlert
Plant physiology, 84(3), 830-834 (1987-07-01)
Ketose reductase (NAD-dependent polyol dehydrogenase EC 1.1.1.14) activity, which catalyzes the NADH-dependent reduction of fructose to sorbitol (d-glucitol), was detected in developing maize (Zea mays L.) endosperm, purified 104-fold from this tissue, and partially characterized. Product analysis by high performance
