Abstract
This chapter focuses on inorganic pyrophosphatases that are described to require Mg 2+ for their action. Inorganic pyrophosphatases have been found in yeast, rat brain, erythrocytes, insect muscle, and potatoes. The orthophosphate formed is determined colorimetrically by the method of Fiske and Subbarow. Inorganic pyrophosphatase from yeast has a very high affinity for its substrate and the pH optimum is 7. In the analysis of pure pyrophosphate solutions it is sufficient to inactivate the enzyme by the addition of the acid molybdate solution. The denatured protein is left in the mixture because it does not interfere with the color reaction. None of the glycolytic enzymes contained in the sample interfere with the determination. Inorganic pyrophosphatase is absolutely specific for inorganic pyrophosphate.
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