Association of inorganic-pyrophosphatase activity with human alkaline-phosphatase preparations

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Abstract
Thi inorganic-pyrophosphatase activity of alkaline phosphatases prepared from human liver and small intestine was investigated at different stages of purification. Both liver and intestinal preparations possessed pyrophosphatase activity at all stages of purification, and the 2 types of activity were not separated by gel filtration or by anion-exchange or cation-exchange chromatography. After starch-gel electrophoresis of the tissue extracts, the zones of pyrophosphatase activity coincided exactly with alkaline-phosphatase zones. Hydrolysis of each type of substrate was inhibited by the presence of the other, and a constant ratio of alkaline-phosphatase activity to pyrophosphatase activity was maintained during inactivation of the enzymes by incubation at 55[degree]. These results are consistent with the view that alkaline phosphatases are also inorganic pyrophosphatases.