The action of cabbage-leaf phospholipase D upon lysolecithin

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Abstract
The action of the water-soluble phosphlipase D from Savoy cabbage leaves upon an aqueous solution of lysolecithin has been studied. Optimum conditions required the presence of Ca2+ ions and pH 5.8. Equivalence was found between the amounts of lysolecithin hydrolyzed and free choline released. The reaction was not accompanied by deacylation. As the enzymic degradation proceeded, and opalescence developed, owing to the insolubility of the reaction product in the presence of Ca2+ ions. Evidence has been obtained indicating the heterogeneity of this reaction product.