Portal de Periódicos da CAPES

The activity of pure phospholipase A2 from Crotalus atrox venom on myelin and on pure phospholipids

1974; Elsevier BV; Volume: 337; Issue: 1 Linguagem: Inglês

10.1016/0005-2760(74)90041-1

1879-145X

Eric Coles, D. L. McIlwain, Maurice M. Rapport,

Ion channel regulation and function

1. Pure phospholipase A2 was prepared from Crotalus atrox venom, in good yield, by DEAE-cellulose chromatography and preparative acrylamide gel electrophoresis. 2. The hydrolytic activity of the enzyme on different substrates was determined in aqueous and diethyl ether media. In the diethyl ether medium, the relative rates of hydrolysis were phosphatidylcholine > phosphatidalcholine > phosphatidylserine ≈ phosphatidalethanolamine > phosphatidylethanolamine, whereas in the aqueous medium, the relative rates were phosphatidylcholine > phosphatidylethanolamine > phosphatidylserine ≈ phosphatidalethanolamine ≈ phosphatidalcholine. 3. In its action on central nervous system myelin the phospholipase showed a preference for phosphatidylethanolamine over phosphatidalethanolamine. The relative rates of hydrolysis of phosphoglycerides in the membrane were phosphatidylserine > phosphatidylcholine > ethanolamine phosphoglycerides. The products (fatty acid and lysophosphatide) remained associated with the membrane after enzyme action.