P5538
Phosphoglucose-Isomerase aus Bacillus stearothermophilus
lyophilized powder, 300-1,000 units/mg protein
Synonym(e):
D-Glucose-6-phosphate ketol-isomerase, PGI, Phosphosaccharomutase
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About This Item
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
300-1,000 units/mg protein
Mol-Gew.
189 kDa
Zusammensetzung
Protein, ≥60% biuret
Lagertemp.
−20°C
Allgemeine Beschreibung
The enzyme is part of the glycolytic pathway. Also, it is important in the industrial production of fructose 1,6-diphosphate (FDP) from glucose. The molecular mass is found to be approximately 189 kDa and it consists of four subunits, each with a molecular mass of approximately 50 kDa. Optimum pH is found to be between 9-10 and the isoelectric point is 4.2.
Anwendung
Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. It is used in sugar assays to convert fructose to glucose. This product is from Bacillus stearothermophilus.
The enzyme from Sigma has been used in the determination of fructose 6-phosphate in a mutant strain of Rhizobium meliloti.
Biochem./physiol. Wirkung
Phosphoglucose Isomerase fuctions as an isomerase, neuroleukin, autocrine motility factor, and a differentiation and maturation mediator.
Einheitendefinition
One unit will convert 1.0 μmole of D-fructose 6-phosphate to D-glucose 6-phosphate per min at pH 9.0 at 30 °C.
Physikalische Form
lyophilized powder containing Tris buffer
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Analysenzertifikate (COA)
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A Arias et al.
Journal of bacteriology, 137(1), 409-414 (1979-01-01)
A mutant strain of complex phenotype was selected in Rhizobium meliloti after nitrosoguanidine mutagenesis. It failed to grow on mannitol, sorbitol, fructose, mannose, ribose, arabitol, or xylose, but grew on glucose, maltose, gluconate, L-arabinose, and many other carbohydrates. Assay showed
The Kinetics and Mechanism of a Reaction Catalyzed by Bacillus stearothermophilus Phosphoglucose Isomerase.
Widjaja A, et al.
Journal of Fermentation and Bioengineering, 86(3), 324-331 (1998)
Monica Totir et al.
PloS one, 7(2), e32498-e32498 (2012-03-07)
Structural biology and structural genomics projects routinely rely on recombinantly expressed proteins, but many proteins and complexes are difficult to obtain by this approach. We investigated native source proteins for high-throughput protein crystallography applications. The Escherichia coli proteome was fractionated
Esdenka Perez et al.
Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 13, 116-123 (2012-10-11)
In the Gran Chaco region the reinfestation by Triatoma infestans remains a major problem for control of Chagas disease. Trypanosoma cruzi the agent of the illness presents a broad genetic intraspecific variability which is poorly documented in the Bolivian Gran
Simone Frédérique Brenière et al.
PLoS neglected tropical diseases, 6(5), e1650-e1650 (2012-06-12)
The current persistence of Triatoma infestans (one of the main vectors of Chagas disease) in some domestic areas could be related to re-colonization by wild populations which are increasingly reported. However, the infection rate and the genetic characterization of the
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