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P3397

Sigma-Aldrich

Phosphoglucomutase from rabbit muscle

ammonium sulfate suspension, ≥100 units/mg protein

Synonyme(s) :

PGM, α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

rabbit muscle

Description

ammonium sulfate suspension, >=100 units/mg protein

Forme

ammonium sulfate suspension

Activité spécifique

≥100 units/mg protein

Conditions de stockage

(Tightly closed)

Technique(s)

activity assay: suitable

Couleur

white to light yellow

Activité étrangère

lactic dehydrogenase ≤0.5%
phosphoglucose isomerase ≤0.01%
pyruvate kinase ≤0.05%

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Description générale

Research area: Cell Signaling

Phosphoglucomutase (PGM), a conserved enzyme, is abundantly found in animals, plants, and microorganisms. It is distributed in almost all tissues.

Application

Phosphoglycomutase has been used:

  • to study glycogenesis and phosphoglycomutase deficiency in humans
  • in phosphoglucomutase assays to study metabolic regulation
  • for assay A to assay enzymes closely linked to glycogen metabolism in transformed BL21(DE3)C43 cells
  • in sucrose synthase (SuSy) andADPglucose pyrophosphorylase (AGPase) assays(3)
  • in enzyme activity assay for coupling the reduction of nicotinamide adenine dinucleotide phosphate (NADP+)to determine glucose-1-phosphate from sucrose and inorganic phosphate (Pi)

Actions biochimiques/physiologiques

Phosphoglucomutase(PGM) enzyme plays a vital role in glycolysis and gluconeogenesis. It is involved in glycogen and trehalose metabolism in insects. PGM participates in the development of plants and some microorganisms. It is essential for proteins, lipids, and nucleic acid metabolism and is crucial for the development of plants because glucose-6-phosphate is a crucial central metabolite. PGM catalyzes the interconversion of glucose-6-phosphate (G-6-P)and glucose-1-phosphate (G-1-P).

Définition de l'unité

One unit will convert 1.0 μmole of α-D-glucose 1-phosphate to α-D-glucose 6-phosphate per min at pH 7.4 at 30 °C.

Forme physique

Crystalline suspension in 3.2 M (NH4)2SO4, pH 6.0 containing 0.01% EDTA

Remarque sur l'analyse

Protein determined by biuret.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

M B Dworkin et al.
The Journal of biological chemistry, 262(35), 17038-17045 (1987-12-15)
When 32P-labeled phosphoenolpyruvate is injected into Xenopus laevis oocytes, a 50-60-kDa protein of subunit size Mr 29,000 is rapidly labeled, followed by a second (monomeric) protein of 66 kDa concomitant with the loss of label from the first protein. We
Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in Escherichia coli
Lee Ha J, et al.
Enzyme and Microbial Technology, 39, 612-620 (2006)
Nora Alonso-Casajús et al.
Journal of bacteriology, 188(14), 5266-5272 (2006-07-04)
To understand the biological function of bacterial glycogen phosphorylase (GlgP), we have produced and characterized Escherichia coli cells with null or altered glgP expression. glgP deletion mutants (DeltaglgP) totally lacked glycogen phosphorylase activity, indicating that all the enzymatic activity is
H Sugie et al.
Neurology, 38(4), 602-605 (1988-04-01)
We report a 5-month-old boy with recurrent vomiting, lethargy, and poor weight gain. He had profound metabolic acidosis and nonketotic dicarboxylic aciduria. The serum and muscle carnitine levels were significantly low (60% and 10% of the control means, respectively), suggesting
Phosphoglucomutase; mechanism of action.
V JAGANNATHAN et al.
The Journal of biological chemistry, 179(2), 569-575 (1949-06-01)

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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