Purification and properties of a lysolecithinase from pancreas

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Abstract
Methods for the detn. of lysolecithinase activity are descr. These are based on the decrease in ester content, measured by a hydroxamic acid reaction, and on the formation of glycerophosphorylcholine, measured by the choline liberated by acid hydrolysis. A procedure is descr. by which the pancreas enzyme is purified 25 times with a reasonable yield (30%). A crystalline prepn. was obtained in low yields, with a specific activity 40 times that of the original extract. Optimum activity was found at pH 6.0 and at a substrate concn. varying from 3-8 [mu] moles/ml. The enzyme does not attack lecithin and triolein.

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