Abstract
Pure venom from the acontial nematocysts of the sea anemone Aiptasia pallida exhibited phospholipase A (phosphatide acyl-hydrolase; EC 3.1.1.4) activity on a mixture of free phospholipids. Diethyl aminoethyl cellulose fractionation of the venom gave four distinct protein peaks with the phospholipase A activity being restricted to fractions III and IV. These two fractions tested separately also were able to lyse red blood cells weakly. Fractions I and II enhanced the hemolytic activity of fractions III and IV, with fractions I and III giving as much as ninefold enhancement over that of III alone. Fraction I appears analogous to the direct lytic factor of some snake and bee venoms. Fraction III, which could not appreciably hydrolyze the phospholipids of the intact red cell membrane, was able to do so in the presence of fraction I. The sequential interactions of these two nematocyst venom proteins with the red blood cell membrane to produce hemolysis is discussed.
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