title: Inorganic pyrophosphatase activity of purified bovine pulp alkaline phosphatase at physiological pH.
abstract: At physiological pH, the hydrolytic activity of purified bovine pulp alkaline phosphatase toward phosphorus compounds was observed to be in the order of inorganic pyrophosphate greater than beta-glycerophosphate greater than phosphorylcholine greater than p-nitrophenylphosphate greater than glucose-6-phosphate. Optimum pH of the enzyme toward inorganic pyrophosphate was shown to be 8.5, with around 60% of the activity at pH 7.5. The activity was increased by the addition of Mg2+, but a different pattern of activation was observed between pH 7.5 and 8.5.
mesh_terms: D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D003782:Dental Pulp / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D043564:Inorganic Pyrophosphatase; D008274:Magnesium / Q000008:administration & dosage / Q000494:pharmacology; D011755:Pyrophosphatases / Q000378:metabolism*
chemical_list: D000469:Alkaline Phosphatase; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D008274:Magnesium