SRE0069
Phosphoglucomutase from rabbit muscle
Sinonimo/i:
α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase
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About This Item
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.32
Prodotti consigliati
Stato
lyophilized powder
Livello qualitativo
Attività specifica
≥100 units/mg protein
Attività estranea
Lactic dehydroenase ≤0.5%
Phosphoglucose Isomerase ≤0.01%
pyruvate kinase ≤0.05%
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
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Descrizione generale
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.
Applicazioni
Phosphoglucomutase from rabbit muscle may be used in dephosphorylation to investigate the hexose bisphosphate activation of phosphoglucomutase.
Azioni biochim/fisiol
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.
Definizione di unità
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.
Stato fisico
Lyophilized powder containing Tris HCl, EDTA, magnesium acetate and carbohydrate
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
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I clienti hanno visto anche
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
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
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