Additional evidence for a lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2.
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Biomedical subjects
Publications and source records attributed to E Condrea.
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The anticoagulant effects and the simultaneous plasma phospholipid hydrolysis induced by three purified phospholipases obtained from snake venoms, i.e., the basic, relatively toxic N. nigricollis, the neutral, relatively nontoxic H. haemachatus, and the acidic, relatively nontoxic N. n. atra, have been compared. The N. nigricollis phospholipase has a very strong anticoagulant effect at concentrations which induce relatively low levels of phospholipid hydrolysis in plasma. The H. haemachatus and N. n. atra phospholipases become anticoagulant only at high concentrations, and the associated phospholipid hydrolysis is also very high. It is concluded that, while all phospholipases are likely to inhibit coagulation if used in amounts sufficiently large to deplete plasma of phospholipids, strongly active phospholipases, such as N. nigricollis, interfere nonenzymatically with the clotting process before any appreciable phospholipid hydrolysis is reached.
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Red cells and membranes prepared from them were treated with graded amounts of palmitoyl, myristoyl and lauroyl lysolecithins. There was no release of phospholipids from the intact red cells in the absence of hemolysis. The solubilization pattern of lipid and protein from the red cell membranes by lysolecithins varies with their chain length.
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Integral and peripheral protein fractions from human red cells membranes were recombined with a total red cell lipid extract and with homologous lipids in varying mixtures, by dialysis from 2-chlorethanol solutions. The 2 protein fractions were compared for lipid binding capacity and for selectivity towards individual lipids.
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