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Merck

P3397

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:
9001-81-4
UNSPSC Code:
12352204
NACRES:
NA.54
Numéro CE :
5.4.2.2 (BRENDA, IUBMB)
MDL number:
MFCD00131886

Nom du produit

Phosphoglucomutase from rabbit muscle, ammonium sulfate suspension, ≥100 units/mg protein

biological source

rabbit muscle

description

ammonium sulfate suspension, >=100 units/mg protein

form

ammonium sulfate suspension

specific activity

≥100 units/mg protein

storage condition

(Tightly closed)

technique(s)

activity assay: suitable

color

white to light yellow

foreign activity

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

shipped in

wet ice

storage temp.

2-8°C

Quality Level

300

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Analysis Note

Protein determined by biuret.

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)

Biochem/physiol Actions

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).

General description

Research area: Cell Signaling

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

Other Notes

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.

Physical form

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

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Certificats d'analyse (COA)

Lot/Batch Number
0000497200
0000497200
0000504274
0000504274
0000477221

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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)
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
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
Phosphoglucomutase; mechanism of action.
V JAGANNATHAN et al.
The Journal of biological chemistry, 179(2), 569-575 (1949-06-01)
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