Abstract
AbstractA synaptic‐membrane fraction rich in junctional components and Na‐K ATPase and AChE activity was isolated from the cerebral cortex of the squirrel monkey. Incubation of membrane preparations with phospholipase C decreased the activity of Na‐K ATPase by 50 per cent but had no effect on the activity of AChE. Analysis of the membrane fraction showed that phospholipase C cleaved both choline phosphoglyceride and the diacyl type of ethanolamine phosphoglyceride from membrane lipids. Addition of egg lecithin at low concentrations partially restored the activity of Na‐K ATPase. Kinetic studies revealed that treatment with phospholipase C may produce a non‐competitive type of inhibition as a result of the cleavage of a charged phosphorylated nitrogen base from membrane lipids.
Published Version
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