Kanfer J N, McCartney D
Department of Biochemistry, University of Manitoba, Winnipeg, Canada.
Neurochem Res. 1990 Oct;15(10):987-92. doi: 10.1007/BF00965744.
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.
