Aldolase

Aldolase is present in all animal and plant tissue and in most microorganisms. Class I aldolase, found in animal and higher plant tissue, is characterized by not requiring a bivalent metal cofactor and by the formation of a ketimine Schiff base intermediate with the substrate dihydroxyacetone phosphate. (This base may be reduced by NaBH4 and the enzyme inactivated). Class II aldolase, found in primitive cells, such as yeast and bacteria, requires a metal cofactor and is inhibited by EDTA.\n\nActivity:\n(same/more than)8u/mg\n\nUnit Definition:\n1 unit will convert 1 micromole of Fructose-1,6-Diphosphate to Dihydroxyacetone phosphate and glyceraldehyde-3-phosphate per min at pH 7.4, 25C.\n\nEnzymatic Impurities:\nPyruvate Kinase: (same/less than)0.1%\nLactic Dehydrogenase: (same/less than)0.03%\nGAPD: (same/less than) .03%\nPhosphoglucose Isomerase: (same/less than)0.6%\nTriosephosphate Isomerase: (same/less than)0.05%\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 6 months at -20 degrees C. Reconstitute with sterile ddH2O immediately before use. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A1335

Size

500U

Form

Supplied as a white lyophilized powder

Purity

~ 80%

References

1. Donovan, J., The Spectrophotometric Titration of the Sulfhydryl and Phenolic Group of Aldolase. Biochem. 3: 67 (1964). 2. Jagannathan, V., Sing, K., Damodaran, M., Carbohydrate Metabolism in Citric Acid Fermentation. IV. Purification and Properties of Aldolase from Aspergillis niger. Biochem. J. 63: 94 (1956). 3. Taylor, J., Aldolase from Muscle in Methods in Enzymology, I, (Colowick, S., and Kaplan, N., eds.) Academic Press, NY: 310 (1955).

Alternative Names

EC=4.1.2.13; Rabbit Muscle