White needle-like crystals or lyophilized powder, soluble in water, pI 6.1, optimum pH 7.0. Stability: dry powder can be stored for one year at 4 ℃; the commercial product is a suspension of 3.2 mol/L ammonium sulphate solution, which can be stable for six months at 4 ℃. Inhibitors are metal ions (Cu2+, Ag+, Zn2+), iodine, o-phenanthroline, adenosine nucleoside phosphate (ATP> ADP> AMP), pyridoxal phosphate, D-arachidonitol-1,5-bisphosphate (KI=1.5 μmol/L), urea (4 mol/L) N-bromide acetoacethanol ammonium. Enzyme reaction: D-fructose-1,6-bisphosphate ═dihydroxyacetone phosphate + D-glyceraldehyde-3-phosphate.
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 . Product A2714 is essentially sulfate-free and contains citrate buffer salts.
An enzyme present in muscle involved in glycogenolysis and anaerobic glycolysis. It catalyzes production of dihydroxyacetone phosphate and phosphoglyceric aldehyde from fructose-1,6-diphosphate.
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 interaction with Wiskott-Aldrich syndrome protein (WASP) may modulate actin dynamics. It reverses the inhibition elicited by ascorbate on Muscle-type LDH (LDH-m4).
