Tsujita T, Okuda H, Yamasaki N
Biochim Biophys Acta. 1982 Apr 13;715(2):181-8. doi: 10.1016/0304-4165(82)90357-9.
Carboxyl ester hydrolase was obtained from rat epididymal adipose tissue in an electrophoretically homogeneous form. Purification was achieved by acetone precipitation, followed by successive chromatographies on DEAE-cellulose and hydroxyapatite and then isoelectric focusing. The monomeric molecular weight of the enzyme was 65,000 and the enzyme associated to form trimers. The enzyme had an isoelectric point at pH 5.9 and contained 2.1% carbohydrate moiety per protein with a molecular weight of 65,000. The amino terminal residue of the enzyme was glycine. The enzyme catalyzed the hydrolysis of short chain triacylglycerols such as tributyrin and medium chain monoacylglycerols such as monocaprin, but not the hydrolysis of cholesterol ester. The optimum pH for the enzymatic function of this enzyme for methyl butylate was 8.0. An antibody against the highly purified enzyme preparation induced in rabbits strongly inhibited the esterase of rat adipose tissue, but did not inhibit the esterase of rat liver, intestinal mucosa and serum.
羧基酯水解酶以电泳纯的形式从大鼠附睾脂肪组织中获得。通过丙酮沉淀进行纯化，随后依次在DEAE - 纤维素和羟基磷灰石上进行层析，然后进行等电聚焦。该酶的单体分子量为65,000，且酶会结合形成三聚体。该酶的等电点为pH 5.9，每65,000分子量的蛋白质含有2.1%的碳水化合物部分。该酶的氨基末端残基为甘氨酸。该酶催化短链三酰甘油（如三丁酸甘油酯）和中链单酰甘油（如单癸酸甘油酯）的水解，但不催化胆固醇酯的水解。该酶对丁酸甲酯的酶促功能的最适pH为8.0。在兔中诱导产生的针对高度纯化酶制剂的抗体强烈抑制大鼠脂肪组织的酯酶，但不抑制大鼠肝脏、肠黏膜和血清的酯酶。
