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G6751

Sigma-Aldrich

α-Glycerophosphate Dehydrogenase from rabbit muscle

Type I, ammonium sulfate suspension, 100-300 units/mg protein

Synonym(s):

sn-Glycerol-3-phosphate Dehydrogenase from rabbit muscle, sn-Glycerol-3-phosphate:NAD+ 2-oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

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

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General description

α-Glycerophosphate dehydrogenase is a membrane protein and a flavin-linked primary dehydrogenase.

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.

Unit Definition

One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.

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.

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Description
Pricing

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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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)
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
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
Tiia Kittilä et al.
Chembiochem : a European journal of chemical biology, 17(7), 576-584 (2016-01-12)
Nonribosomal peptide synthetases (NRPSs) produce many important and structurally complex natural products. Because of their architectures, reprogramming NRPSs has long been attempted to access new bioactive compounds. However, detailed characterization of NRPS catalysis and substrate selectivity by adenylation (A) domains
Talia Miron et al.
European journal of medicinal chemistry, 45(5), 1912-1918 (2010-02-06)
Allylsulfides from garlic are chemopreventive agents. Entering cells they are expected to initially interact with glutathione. Accordingly, reaction mechanisms of the product, S-allylthio-glutathione, with model proteins and thiols were analyzed in cell free systems. With glutathionyl, cysteinyl or captopril representing

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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