Abstract
Two forms of Ca 2+-independent cytosolic phospholipases A 2 were separated by Sephadex G-75 column chromatography. N-Acetylneuraminic acid, gangliosides, and sialoglycoproteins inhibited both phospholipases A 2 in a concentration dependent manner, but colominic acid, poly(2,8-N-acetylneuraminic acid), had no effect on enzymic activities. Interactions between phospholipases A 2 and sialoglycoconjugates may be involved in the translocation of phospholipases A 2 from cytosol to plasma membrane during receptor stimulation.
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Schedule a callMore From: Biochemical and biophysical research communications
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