Mechanism of the Ether Activation of Phospholipase A

Abstract

IT has recently been shown that with many phospholipases the rate of reaction is appreciably influenced by the electrokinetic state of the enzyme and its substrate. Thus the lecithin-splitting activity of the phospholipase B of Penicillium notatum requires a negative ζ potential on the substrate's surface before activity commences, while the phospholipase C from Cl. perfringens needs a negatively charged enzyme and excess positive groups on the substrate^1,2. On the other hand, the triphospho-inositide phosphomonoesterase of brain³ requires the negative ζ potential of the substrate to be considerably reduced before activity can begin at an appreciable rate.