Lombardo D, Guy O, Figarella C
Biochim Biophys Acta. 1978 Nov 10;527(1):142-9. doi: 10.1016/0005-2744(78)90263-2.
A carboxyl ester hydrolase has been purified 20-fold from human pancreatic juice. It is a glycoprotein with a molecular weight of 100 000. It contains 9% neutral and amino carbohydrates and the amino acid composition is characterized by a high content of proline residue (12.7%). The enzyme catalyzes the hydrolysis of p-nitrophenylacetate and the activity increases in the presence of biliary salts; V is not modified but Km is decreased 10 times by addition of biliary salts. The enzyme migrates on Sephadex G-200 as a protein with a molecular weight of 300 000. This behaviour does not seem to be due to a polymerization but to a peculiar configuration of the enzyme.
一种羧基酯水解酶已从人胰液中纯化了20倍。它是一种糖蛋白，分子量为100000。它含有9%的中性和氨基碳水化合物，氨基酸组成的特点是脯氨酸残基含量高（12.7%）。该酶催化对硝基苯乙酸的水解，在胆汁盐存在下活性增加；V不变，但加入胆汁盐后Km降低10倍。该酶在Sephadex G-200上迁移时表现为分子量为300000的蛋白质。这种行为似乎不是由于聚合作用，而是由于酶的特殊构型。
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