Tsujita T, Okuda H
Eur J Biochem. 1983 Jun 1;133(1):215-220. doi: 10.1111/j.1432-1033.1983.tb07450.x.
The three enzyme activities, carboxylesterase, aryl acylamidase and cholinesterase activities, have been found in rat and human sera. Rat serum carboxylesterase associated with serum aryl acylamidase activity, but not with serum cholinesterase activity, was purified by ammonium sulfate precipitation, followed by successive chromatographies on DEAE-cellulose, blue Sepharose and QAE-Sephadex, and then electrophoresis. Evidence for the identity of the two enzymes, carboxylesterase and aryl acylamidase, was their co-elution profiles and co-purification in the different steps, including electrophoresis, with constant ratios of specific activities and percentage recoveries. Human serum carboxylesterase associated with serum cholinesterase, purified earlier, was compared with the rat serum esterase. Human serum carboxylesterase and aryl acylamidase activities were inhibited by serotonin and neostigmine, whereas rat serum carboxylesterase and aryl acylamidase activities were not affected by these compounds. Tyramine activated human but not rat aryl acylamidase. Rat and human serum esterase activities were both strongly inhibited by the diisopropylfluorophosphate. Both esterases 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.
在大鼠和人血清中发现了三种酶活性，即羧酸酯酶、芳基酰胺酶和胆碱酯酶活性。通过硫酸铵沉淀，随后依次在DEAE - 纤维素、蓝色琼脂糖和QAE - 葡聚糖上进行色谱分离，然后进行电泳，纯化了与血清芳基酰胺酶活性相关但与血清胆碱酯酶活性无关的大鼠血清羧酸酯酶。羧酸酯酶和芳基酰胺酶这两种酶同一性的证据在于它们在不同步骤（包括电泳）中的共洗脱图谱和共纯化，其比活性和回收率百分比保持恒定。将先前纯化的与人血清胆碱酯酶相关的人血清羧酸酯酶与大鼠血清酯酶进行了比较。血清素和新斯的明可抑制人血清羧酸酯酶和芳基酰胺酶活性，而这些化合物对大鼠血清羧酸酯酶和芳基酰胺酶活性没有影响。酪胺可激活人而非大鼠的芳基酰胺酶。大鼠和人血清酯酶活性均受到二异丙基氟磷酸的强烈抑制。两种酯酶都催化短链三酰甘油（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。
