Aldolase, MP Biomedicals

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0215985925 0215985980
IC15985925EA 131.49 USD
IC15985925 IC15985980
Aldolase, MP Biomedicals
Enzymes

One unit is the change in absorbancy of 1.00 per minute at 25 °C, pH 7.5.


Inhibitors: Aldolase in inhibited by Cu2+, Ag+, Zn2+ and o-phenanthroline. It is inactivated by N-bromoacetylethanolamine phosphate5 and pyridoxal phosphate. Stability: Aldolase is irreversibly denatured at pH values less than 4.5.


Aldolase is a tetrameric protein. It catalyzes a key reaction in glycolysis and energy production:D-Fructose 1,6-bisphosphate Aldolase> dihydroxyacetone phosphate + D-glyceraldehyde-3-phosphate. Aldolase is present in all animal tissue and in most microorganisms. There are two classes of aldolases. Class I aldolase is found in animal and higher plant tissue. Class II aldolase is found in primitrive cells such as yeasts and bacteria. Class I aldolase is characterized by not requiring a bivalent metal cofactor and the formation of a ketimine Schiff base intermediate with the substrate dihydroxyacetone phosphate. Class II aldolase requires a metal cofactor and is inhibited by EDTA. Three types of aldolase exist in animal tissue. The major form, type A is found in muscle; type B is found in liver tissue and type C (plus some type A) is found in brain tissue. Aldolase forms five isozymes which may to various degrees be organ specific.


Aldolase is used in an hydrazine assay based on Boyer's modification in which 3-phosphoglyceraldehyde reacts with hydrazine to form a hydrazone which absorbs at 240 nm.

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