Phospholipases. II. Enzymatic hydrolysis of lecithin: Effects of structure,cholesterol content,and sonication

Summary Hydrolysis of unsonicated liposomes of egg lecithin catalyzed by several phospholipases is markedly activated by addition ofn-alkanols Jain & Cordes,J. Membrane Biol. 14:101 (1973)]. Further pursuit of these systems has established that several factors, including higher temperatures, increasing unsaturation of fatty acyl chains of the substrate, incorporation of cholesterol into the liposomes, and sonication, reduce the concentration ofn-hexanol required to elicit maximal activation for enzymatic hydrolysis. Moreover, sonication or incorporation of cholesterol into lecithin liposomes reduces from C₈ to C₇ and C₆, respectively, the chain length of that alcohol eliciting maximal activation. These results are consistent with the hypothesis that sonication and increasing cholesterol content lead to liposomes which have a diminished thickness of the hydrocarbon region compared to that for unmodified liposomes derived from the same lecithin.