The enzymic hydrolysis of phosphatides

Abstract

An enzyme (lecithinase) contained in kidney and in intestinal mucosa hydrolysed lecithin from several sources with the liberation of phosphoric acid. It acted most rapidly at body temp., and had an optimum pH of 7.5. Hydrolecithin was attacked by the enzyme as fast as its parent lecithin, kephalin and phosphatidic acid somewhat more slowly, the latter showing no marked dependence on pH. Synthetic lecithin and distearyl phosphate were attacked at a lower rate and without showing any pH optima. Lysolecithin was hydrolysed about twice as fast as lecithin. Brominated lecithin was hydrolysed at a much greater rate than lecithin. This may have been due to the greater negativity of the alcohol part of the ester due to the introduction of several bromine atoms in the side chain. Certain anomalies in the enzymic rates of hydrolysis suggested that synthetic lecithin and the natural product might not have the same chemical configuration.