An unusual phosphodiesterase activity towards p-nitrophenylphosphorylcholine present in rat brain membranes.
A phosphodiesterase activity present in rat brain membranes has been examined utilizing p-nitrophenylphosphorylcholine as the substrate. This enzyme activity has a pH optimum of 8.5, is stimulated by a variety of free fatty acids, requires either Zn+2 or Ca+2 and is relatively stable to heating at 75 degrees C for 7.5 minutes. These properties appear to distinguish this particular activity from those previously reported for alkaline phosphatase, nonspecific phosphodiesterase, phosphodiesterases I and II, lecithinase, and sphingomyelinase.
Kanfer
J N
JN
Department of Biochemistry, University of Manitoba, Winnipeg, Canada.
McCartney
D
D
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002413:Cations, Divalent; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology; D003902:Detergents / Q000494:pharmacology; D005230:Fatty Acids, Nonesterified / Q000494:pharmacology; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity; D014461:Ultracentrifugation
C033523:4-nitrophenylphosphorylcholine; D002413:Cations, Divalent; D003902:Detergents; D005230:Fatty Acids, Nonesterified; D010767:Phosphorylcholine; D010727:Phosphoric Diester Hydrolases