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Merck

A8811

Aldolase from rabbit muscle

ammonium sulfate suspension, 10-20 units/mg protein

Synonyme(s) :

D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Numéro CE :
MDL number:
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Nom du produit

Aldolase from rabbit muscle, ammonium sulfate suspension, 10-20 units/mg protein

biological source

rabbit muscle

form

ammonium sulfate suspension

specific activity

10-20 units/mg protein

foreign activity

glyceraldehyde-3-phosphate dehydrogenase ≤0.03%
lactic dehydrogenase ≤0.03%
phosphoglucose isomerase ≤0.6%
pyruvate kinase ≤0.1%
triosephosphate isomerase ≤0.05%

storage temp.

2-8°C

Quality Level

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Analysis Note

Protein determined by biuret.

Application

Aldolase from rabbit muscle has been used:
  • in standard 1-phosphofructokinase from rabbit muscle (RPFK-1) assay
  • as a standard in the characterization of metabolic enzymes from glaucomatous tissues
  • in fructose 2,6-bisphosphate assay of human cell lines

Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Aldolase, from rabbit muscle has been used for stereospecific deprotonation at DHAP C3 .

Biochem/physiol Actions

Aldolase interaction with Wiskott-Aldrich syndrome protein (WASP) may modulate actin dynamics. It reverses the inhibition elicited by ascorbate on Muscle-type LDH (LDH-m4).
Aldolase is involved in gluconeogenesis, the Calvin cycle and glycolysis. Aldolase, from rabbit muscle, is a class I aldolase which forms covalent Schiff base intermediates. The active site of aldolase is in the center of the α/β 8 barrel fold .

General description

Aldolase exists as three isoforms in rabbit, which includes type A from muscle, type B from liver and brain associated type C. Aldolases correspond to a molecular weight of 158 kDa and exists as tetramer.

Other Notes

One unit will convert 1.0 μmole of fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate per min at pH 7.4 at 25 °C.

Physical form

Crystalline suspension in 2.5 M (NH4)2SO4, 0.01 M Tris, pH 7.5, 0.001 M EDTA

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Consulter la Bibliothèque de documents

Effect of lithium salts on lactate dehydrogenase, adenylate kinase, and 1-phosphofructokinase activities
Russell P, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry, 25(4), 551-556 (2010)
Structure of rabbit muscle aldolase at low resolution.
Sygusch J, et al.
The Journal of Biological Chemistry, 260(28), 15286-15290 (1985)
A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein
St-Jean M, et al.
The Journal of biological chemistry, 282(19), 14309-14315 (2007)
Clotilde LowKam et al.
The Journal of biological chemistry, 285(27), 21143-21152 (2010-04-30)
Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four
Linjun Guo et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 8), 958-961 (2012-08-08)
4-Hydroxy-3-methyl-2-keto-pentanoate aldolase (asHPAL), an enzyme used in the synthesis of (2S,3R,4S)-4-hydroxyisoleucine, was crystallized in the absence and the presence of 2-ketobutyrate as one of its substrates by the sitting-drop vapour-diffusion method using PEG 400 as a precipitant. Crystals of asHPAL

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