Inhibition of the orthophosphatase and pyrophosphatase activities of human alkaline-phosphatase preparations |
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Authors: | Eaton R H Moss D W |
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Institution: | University Department of Clinical Chemistry, The Royal Infirmary, Edinburgh, 3. |
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Abstract: | 1. Purified human liver and small-intestinal alkaline orthophosphatases release inorganic phosphate at appreciable rates from a variety of organic pyrophosphate substrates. 2. The pyrophosphatase action is inhibited by Mg2+ ions at concentrations that activate the hydrolysis of orthophosphate substrates by these enzymes. 3. The results of mixed-substrate experiments, denaturation studies with heat or urea and starch-gel electrophoresis suggest that both orthophosphatase and pyrophosphatase activities are, in each preparation, properties of a single enzyme. 4. Intestinal phosphatase shows greater pyrophosphatase activity relative to orthophosphatase than the liver enzyme. |
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