Inhibition of phospholipase A2 and phospholipase C by polyamines

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Abstract

The polyamines spermine, spermidine, and putrescine inhibit the activity of phospholipase A2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is highest for spermine and lowest for putrescine. With both enzymes, inhibition is stronger when phospholipid vesicles rather than mitochondrial membranes are used as the substrate. No clear competition of polyamines with Ca2+, which is required for the activity of both enzymes, has been observed. The inhibition appears to be due to steric hindrance of enzyme-substrate interaction due to the binding of the organic polycations to the phospholipid bilayer.

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    Present address: Istituto di Biochimica, Universitá di Ancona, Italy.

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