A LECITHINASE A IN DUODENAL CONTENTS OF MAN

Open Access
Publisher Website
Google Scholar
Abstract
A lecithinase A was demonstrated in the duodenal contents of man. The release of fatty acids from lecithin was measured titrimetricaUy. The decrease in lecithin and equivalent increase in lysolecithin were determined independently by quantitative paper chromatography. The action of the enzyme was markedly increased in the presence of sodium deoxycholate and moderately increased by glycine, glutamic acid, arginine or lysine. The optimum medium used for the hydrolysis was a glycine-borate buffer at pH 8.5, and the optimum temperature was 55[degree] C. Heating in this medium at 80[degree] C for 30 minutes did not inactivate the enzyme. The enzyme was partially inhibited by Ca, Mg, oxalate, oleic acid, and diethyl ether, and nearly completely inhibited by ethylenediamine tetraacetic acid.