title: The hydrolysis of glycerophosphocholine by rat brain microsomes: activation and inhibition.
abstract: Experiments with glycerophosphocholine phosphodiesterase (GPC diesterase, EC 3.1.4.2.) in rat brain microsomes suggest that, although its activity is inhibited by low concentrations of calmidazolium, its dependence on Ca2+ ions is not modulated by calmodulin. The activity of glycerophosphocholine choline phosphodiesterase (choline phosphohydrolase, EC 3.1.4.38) was much lower than that of the GPC diesterase. A relatively inexpensive method for the preparation of sn-glycero-3-phospho [Me-14C]choline is described.
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism*; D001923:Brain Chemistry; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000494:pharmacology; D005260:Female; D005997:Glycerylphosphorylcholine / Q000378:metabolism*; D006868:Hydrolysis; D007093:Imidazoles / Q000494:pharmacology; D008861:Microsomes / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D051381:Rats
chemical_list: D002147:Calmodulin; D007093:Imidazoles; C031938:calmidazolium; D005997:Glycerylphosphorylcholine; D010727:Phosphoric Diester Hydrolases; D002118:Calcium