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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
10-20 units/mg protein
Biological source:
rabbit muscle
biological source
rabbit muscle
Quality Level
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
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 .
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.
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.
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Related Content
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)
Structure of rabbit muscle aldolase at low resolution.
Sygusch J, et al.
The Journal of Biological Chemistry, 260(28), 15286-15290 (1985)