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.
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 .
5000 units in glass bottle
100, 200, 1000 units in poly bottle
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 .
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.
Crystalline suspension in 2.5 M (NH4)2SO4, 0.01 M Tris, pH 7.5, 0.001 M EDTA
Protein determined by biuret.