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SRE0069

Sigma-Aldrich

Phosphoglucomutase aus Kaninchenmuskel

Synonym(e):

αα-D-Glucose-1,6-bisphosphatase, αα-D-Glucose-1-phosphatphosphotransferase

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About This Item

CAS-Nummer:
EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32

Form

lyophilized powder

Qualitätsniveau

Spezifische Aktivität

≥100 units/mg protein

Fremdaktivität

Lactic dehydroenase ≤0.5%
Phosphoglucose Isomerase ≤0.01%
pyruvate kinase ≤0.05%

Versandbedingung

wet ice

Lagertemp.

−20°C

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Allgemeine Beschreibung

Research area: CellSignalling. The phosphoglucomutase (PGM) molecule, a single polypeptide chain, is made up of four α/β domains. The domains form a compact heart-shaped structure with a large fissure between the two lobes, and the molecule comprises about 40 secondary structural components. The active enzymatic site of the molecule is located at the bottom of the crevice on the surface of domain I. Rabbit muscle phosphoglucomutase (RB-PGM) is a monomer with a unique four-domain architecture.

Anwendung

Phosphoglucomutase from rabbit muscle may be used in dephosphorylation to investigate the hexose bisphosphate activation of phosphoglucomutase.

Biochem./physiol. Wirkung

Phosphoglucomutase (PGM) mainly catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate via a glucose 1,6-diphosphate intermediate. Hence it plays a key role in glycolysis and gluconeogenesis.

Einheitendefinition

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.

Physikalische Form

Lyophilized powder containing Tris HCl, EDTA, magnesium acetate and carbohydrate

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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S Levin et al.
Protein engineering, 12(9), 737-746 (1999-10-03)
Three-dimensional structural models of three members of the phosphoglucomutase (PGM) superfamily, parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase, were constructed by homology modeling based on the known crystal structure of rabbit muscle phosphoglucomutase. Parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase
C M Galloway et al.
Plant physiology, 79(3), 920-922 (1985-11-01)
The hexose bisphosphate activation of phosphoglucomutase was investigated with both plant (pea and mung bean) and animal (rabbit muscle) sources of the enzyme. Plant phosphoglucomutase was purified about 50-fold from seeds, and to a lesser extent, from seedlings of Pisum

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