The effect of different molecular species of sphingomyelin on phospholipase C δ1 activity

摘要

Bovine brain sphingomyelin was separated into different molecular species using a reverse phase column. PLCδ1 was inhibited by all molecular species of sphingomyelin. The extent of this inhibition was dependent on the hydrophobicity. Based on fatty acid analysis, we conclude that the inhibition of PLCδ1 depends on the chain length and degree of unsaturation of the fatty acid moiety of SM. N-palmi- toyl-D-sphingomyelin and N-stearoyl-D-sphingomyelin inhibited PLCδ1 less then N-oleoyl-D-sphingomyelin.