Abstract
MORE than 130 compounds have been screened recently for their effect on the activity of rat intestinal alkaline phosphatase1 (EC.3.1.3.1). Some intermediates of the tricarboxylic acid cycle were without effect on the enzyme, but citrate was not included in these tests. In the work recorded here, citrate was found to inhibit intestinal alkaline phosphatase in the absence of added magnesium ions. Assays were performed, in duplicate, by measuring the inorganic phosphate2 liberated from β-glycerophosphate at pH 9.8 (0.05M barbitone), that is, near the pH optimum for this enzyme. A progress curve was linear for an incubation time of 30 min. Hence the experimental time period of 15 min was well within the phase of initial velocity. The enzyme was a commercial purified product prepared from calf intestinal mucosa (L. Light and Co., Ltd.).
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EVERED, D., STEENSON, T. Citrate Inhibition of Alkaline Phosphatase. Nature 202, 491–492 (1964). https://doi.org/10.1038/202491a0
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DOI: https://doi.org/10.1038/202491a0
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Hemmung der sauren Phosphatase aus Rattenleberlysosomen durch Citrat
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