title: A p-nitrophenyl phosphorylcholine phosphodiesterase from mouse brain.
abstract: The phosphodiesterase which catalyzes the hydrolysis of p-nitrophenyl phosphorylcholine was solubilized from mouse brain by 1% sodium deoxycholate treatment, and partially purified by HPLC gel chromatography. The enzyme, tightly bound to membranes and relatively stable, possessed apparent values of Km of 1 mM and Vmax of 150 n moles/mg. hr, and gave optimum pH of 11. Additionally, the molecular weight of the enzyme, EDTA-insensitive and divalent ions-independent, was estimated to be 150,000. Based on these results, this phosphodiesterase is supposed to be different from the phosphodiesterases reported previously.
authors.affiliation: Department of Food & Nutrition, Chungnam National University, Daejeon, Korea.
authors.forename: D E
authors.initials: DE
authors.lastname: Sok
authors.forename: M R
authors.initials: MR
authors.lastname: Kim
mesh_terms: D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002412:Cations / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics; D051379:Mice; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D010261:Paraoxon / Q000494:pharmacology; D010767:Phosphorylcholine / Q000494:pharmacology; D013379:Substrate Specificity; D013574:Synaptosomes / Q000201:enzymology
chemical_list: D002412:Cations; D010767:Phosphorylcholine; D004492:Edetic Acid; D009597:4-Nitrophenylphosphatase; D010261:Paraoxon