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A8811

Sigma-Aldrich

Aldolase from rabbit muscle

ammonium sulfate suspension, 10-20 units/mg protein

Synonym(s):

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

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About This Item

CAS Number:
9024-52-6
Enzyme Commission number:
4.1.2.13 (BRENDA, IUBMB)
MDL number:
MFCD00130453
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

200

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

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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.

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 .

Unit Definition

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

Analysis Note

Protein determined by biuret.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

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Structure of rabbit muscle aldolase at low resolution.
Sygusch J, et al.
The Journal of Biological Chemistry, 260(28), 15286-15290 (1985)
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)
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)
Aldolase and actin protect rabbit muscle lactate dehydrogenase from ascorbate inhibition
Russell PJ, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry, 19(1), 91-98 (2004)
Veronika Ostatná et al.
Analytica chimica acta, 735, 31-36 (2012-06-21)
In an attempt to develop a label-free electrochemical method for detection of changes in protein structures based on oxidizability of tyrosine and tryptophan residues we tested different types of carbon electrodes. We found that using edge plane pyrolytic graphite electrode
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