Phospholipases. III. Effects of ionic surfactants on the phospholipase-catalyzed hydrolysis of unsonicated egg lecithin liposomes

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Abstract
Apparent values ofK m and V max have been measured for catalysis of hydrolysis of unsonicated egg lecithin liposomes, activated through addition of 0.04m n-hexanol, by phospholipases A2 from bee and snake venoms and by phospholipase C fromClostridium welchii as a function of the concentration of three surfactants: hexadecylamine, hexadecyltrimethylammonium bromide, and dihexadecyl phosphate. For all three enzymes, values ofK m andV max show little or no dependence on the concentration of these ionic surfactants, demonstrating that the liposomal surface charge is not a crucial factor in determining susceptibility to phospholipase-catalyzed hydrolysis.