Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids
D Lombardo, J Fauvel, O Guy - Biochimica et Biophysica Acta (BBA) …, 1980 - Elsevier
Purified carboxyl ester hydrolase (carboxylic-ester hydrolase, EC 3.1. 1.1) from human
pancreatic juice was found to hydrolyze triacetin, methyl butyrate and glycerides solubilized
by bile salts. It has no activity on substrate presented as emulsion or monomolecular films.
The human enzyme was found to deacylate phospholipids and lysophospholipids at
different rates. The hydrolysis of short-chain phospholipids and lysophospholipids at
different rates. The hydrolysis of short-chain phosphatidylcholines was dependent of …
pancreatic juice was found to hydrolyze triacetin, methyl butyrate and glycerides solubilized
by bile salts. It has no activity on substrate presented as emulsion or monomolecular films.
The human enzyme was found to deacylate phospholipids and lysophospholipids at
different rates. The hydrolysis of short-chain phospholipids and lysophospholipids at
different rates. The hydrolysis of short-chain phosphatidylcholines was dependent of …