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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-982-3
MDL number:
Specific activity:
100-300 units/mg protein
Biological source:
rabbit muscle
biological source
rabbit muscle
type
Type I
form
ammonium sulfate suspension
specific activity
100-300 units/mg protein
storage condition
(Tightly closed)
technique(s)
activity assay: suitable
color
white
foreign activity
Lactic dehydrogenase, pyruvate kinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%, Triosephosphate isomerase ≤0.02%
storage temp.
2-8°C
Quality Level
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General description
α-Glycerophosphate dehydrogenase is a membrane protein and a flavin-linked primary dehydrogenase.
Research area: Cell Signaling
Research area: Cell Signaling
Application
α-Glycerophosphate Dehydrogenase from rabbit muscle has been used:
- in the reaction mixture to measure the glycerol kinase activity
- to demonstrate compartmentalized enzymatic reactions where NADH is involved
- in the reaction mixture assay for L-fuculose-1-phosphate aldolase
Biochem/physiol Actions
α-Glycerophosphate dehydrogenase catalyzes the oxidation of L-α-glycerophosphate (Glp) to form dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2). This enzyme is associated with respiratory electron transport chain, glycolysis, and phospholipid metabolism.
Physical form
Crystalline suspension in 3.2 M (NH4)2SO4 and 0.1 g/L EDTA solution, pH 6.0
Preparation Note
Prepared by modification of the method of Fondy.
Analysis Note
Protein determined by biuret.
Other Notes
One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Joanne I Yeh et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(9), 3280-3285 (2008-02-26)
Sn-glycerol-3-phosphate dehydrogenase (GlpD) is an essential membrane enzyme, functioning at the central junction of respiration, glycolysis, and phospholipid biosynthesis. Its critical role is indicated by the multitiered regulatory mechanisms that stringently controls its expression and function. Once expressed, GlpD activity
Somchart Maenpuen et al.
The FEBS journal, 282(16), 3043-3059 (2015-02-26)
L-α-glycerophosphate oxidase is an FAD-dependent enzyme that catalyzes the oxidation of L-α-glycerophosphate (Glp) by molecular oxygen to generate dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2). The catalytic properties of recombinant His6-GlpO from Mycoplasma pneumoniae (His6-MpGlpO) were investigated through transient and
Structural studies on nicotinamide adenine dinucleotide-linked L-glycerol 3-phosphate dehydrogenase crystallized from rat skeletal muscle.
T P Fondy et al.
The Journal of biological chemistry, 243(11), 3148-3160 (1968-06-10)
Optimal conditions for biomass and recombinant glycerol kinase production using the yeast Pichia pastoris
Aizemberg R, et al.
Food Technology and Biotechnology, 49(3), 329-329 (2011)
Susan K Boehlein et al.
The Plant journal : for cell and molecular biology, 99(1), 23-40 (2019-02-13)
Cereal yields decrease when grain fill proceeds under conditions of prolonged, moderately elevated temperatures. Endosperm-endogenous processes alter both rate and duration of dry weight gain, but underlying mechanisms remain unclear. Heat effects could be mediated by either abnormal, premature cessation
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