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SRE0069
Phosphoglucomutase aus Kaninchenmuskel
Synonym(e):
αα-D-Glucose-1,6-bisphosphatase, αα-D-Glucose-1-phosphatphosphotransferase
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About This Item
Empfohlene Produkte
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
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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
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
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