Abstract
Snake venom protein was separated into lecithinase A-I and A-II by column chromatography using ion-exchange cellulose and examinations were made on the action of inhibitors on the activity of these enzymes, demand for metal ions, effect of pH on the activity, and the product of substrate decomposition. The decomposition was examined with dipalmitoleyl-L-α-lecithin obtained from yeast and its hydrogenated dipalmitoyl-L-α-lecithin. Lecithinase A-II hydrolyzed both these lecithins to about the same degree but lecithinase A-I hydrolysed only dipalmitoleyl-L-α-lecithin and had only a weak action on dipalmitoyl-L-α-lecithin.
