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83895

Sigma-Aldrich

D-Ribulose 1,5-bisphosphate sodium salt hydrate

≥99.0% (TLC)

Synonyma:

D-erythro-2-Pentulose, 1,5-bis(dihydrogen phosphate), D-Ribulose 1,5-diphosphate, RuDP

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
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About This Item

Empirický vzorec (Hillův zápis):
C5H12O11P2 · xNa+ · yH2O
Číslo CAS:
1897433-92-9
Molekulová hmotnost:
310.09 (anhydrous free acid basis)
UNSPSC Code:
12352201
NACRES:
NA.25

assay

≥99.0% (TLC)

form

powder

color

white

solubility

H2O: 50 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

InChI

1S/C5H12O11P2/c6-3(1-15-17(9,10)11)5(8)4(7)2-16-18(12,13)14/h3,5-6,8H,1-2H2,(H2,9,10,11)(H2,12,13,14)/t3-,5-/m1/s1

InChI key

YAHZABJORDUQGO-NQXXGFSBSA-N

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Související kategorie

Application

Ribulose-1,5-bisphosphate (RuBP) is a component of the Calvin cycle that is metabolized into glycerate 3-phosphate (G3P) by the enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO). RuBP is used to identify, differentiate and characterize ribulose bisphosphate carboxylase(s)/oxygenase(s) (RuBisCO).

Other Notes

To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Active site studies with ribulose-1,5-biphosphate carboxylase

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges

Osvědčení o analýze (COA)

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Navštívit knihovnu dokumentů

S N Mogel et al.
Biochemistry, 28(13), 5428-5431 (1989-06-27)
Irradiation of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach in the presence of vanadate at 4 degrees C resulted in rapid loss of carboxylase activity. The inactivation was light and vanadate dependent. When the enzyme was irradiated in the presence of the substrate
M Sawada et al.
The international journal of biochemistry & cell biology, 32(4), 447-454 (2000-04-13)
6-Phosphofructo-1-kinase and fructose-1,6-bisphosphatase are rate-limiting enzymes for glycolysis and gluconeogenesis respectively, in the fructose 6-phosphate/fructose 1,6-bisphosphate cycle in the liver. The effect of ribose 1,5-bisphosphate on the enzymes was investigated. Ribose 1,5-bisphosphate synergistically relieved the ATP inhibition and increased the
I Ozaki et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 125(1), 97-102 (2000-06-07)
Fructose-1,6-bisphosphatase is one of the regulatory enzymes of gluconeogenesis in kidney cortex. The effect of ribose 1,5-bisphosphate on fructose-1,6-bisphosphatase purified from rat kidney cortex was studied. Rat kidney cortex, fructose-1,6-bisphosphatase exhibited hyperbolic kinetics with regard to its substrate, but the
S Ogushi et al.
The Journal of biological chemistry, 265(19), 10943-10949 (1990-07-05)
The tissue contents of previously known allosteric effectors of brain phosphofructokinase (EC 2.7.1.11) (PFK) and the kinetic behavior of isolated PFK were investigated during the initiation of rapid glycolytic flux in freeze-blown rat brain. Comparing 0- with 5-s brains revealed
Takaaki Sato et al.
Science (New York, N.Y.), 315(5814), 1003-1006 (2007-02-17)
The type III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) present in the archaeon Thermococcus kodakaraensis was found to participate in adenosine 5'-monophosphate (AMP) metabolism, a role that is distinct from that of classical RuBisCOs of the Calvin-Benson-Bassham cycle. Genes annotated as thymidine phosphorylase
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