Tsujita T, Okuda H
J Biochem. 1983 Sep;94(3):793-7. doi: 10.1093/oxfordjournals.jbchem.a134421.
Carboxylesterase was obtained from human liver in an electrophoretically homogeneous form. The monomeric molecular weight of the enzyme was 60,000 and the enzyme associated to form trimers. Purified human liver carboxylesterase was compared with human serum carboxylesterase, purified earlier. Serum carboxylesterase hydrolyzed a typical cholinesterase substrate and aryl acylamide, whereas liver carboxylesterase did not hydrolyze these compounds. Both carboxylesterases catalyzed the hydrolysis of short-chain triacylglycerols, such as tributyrin, and medium-chain monoacylglycerols, such as monocaprin, but not the hydrolysis of long-chain triacylglycerols. Serum carboxylesterase activity was inhibited by p-trimethylammoniumanilinium dichloride and neostigmine, whereas liver carboxylesterase activity was not affected by these compounds. Liver and serum carboxylesterase activities were both strongly inhibited by phenylmethylsulfonyl fluoride.
羧酸酯酶以电泳纯的形式从人肝脏中获得。该酶的单体分子量为60,000，且酶会结合形成三聚体。将纯化的人肝脏羧酸酯酶与先前纯化的人血清羧酸酯酶进行比较。血清羧酸酯酶可水解典型的胆碱酯酶底物和芳基酰胺，而肝脏羧酸酯酶则不能水解这些化合物。两种羧酸酯酶均催化短链三酰甘油（如三丁酸甘油酯）和中链单酰甘油（如单癸酸甘油酯）的水解，但不催化长链三酰甘油的水解。血清羧酸酯酶活性受到对-三甲基铵苯胺二氯化物和新斯的明的抑制，而肝脏羧酸酯酶活性不受这些化合物的影响。肝脏和血清羧酸酯酶活性均受到苯甲基磺酰氟的强烈抑制。
