Lombardo D, Fauvel J, Guy O
Biochim Biophys Acta. 1980 Jan 11;611(1):136-46. doi: 10.1016/0005-2744(80)90049-2.
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 emulsoin or monomolecular films. The human enzyme was found to deacylate phospholipids and lysophospholipids at different rates. The hydrolysis of short-chain phosphatidylcholines was dependent of substrate solubility and dioctanoyl phosphatidylcholine was deacylated with the highest rate. Long-chain phosphatidylcholines and lysophosphatidylcholines present in microsomal membranes were deacylated with very low rates, only lysophosphatidylcholine deacylation was faster. Evidence is presented that human carboxyl ester hydrolase is the lyophosphatidyl-choline-hydrolyzing enzyme corresponding to bovine lysophospholipase. Bile salts play an important part on the activity of human carboxyl ester hydrolase, in addition to the role of detergent that they have on insoluble substrates.
从人胰液中纯化得到的羧基酯水解酶（羧酸酯水解酶，EC 3.1.1.1）被发现可水解三醋精、丁酸甲酯以及被胆盐增溶的甘油酯。它对以乳剂或单分子膜形式存在的底物没有活性。发现人源酶以不同速率使磷脂和溶血磷脂脱酰基。短链磷脂酰胆碱的水解取决于底物的溶解度，二辛酰磷脂酰胆碱脱酰基的速率最高。微粒体膜中存在的长链磷脂酰胆碱和溶血磷脂酰胆碱脱酰基的速率非常低，只有溶血磷脂酰胆碱的脱酰基速率较快。有证据表明，人羧基酯水解酶是与牛溶血磷脂酶相对应的溶血磷脂酰胆碱水解酶。除了作为不溶性底物的去污剂所起的作用外，胆盐对人羧基酯水解酶的活性也起着重要作用。
