Mentlein R, Lembke B, Vik H, Berge R K
Biochem Pharmacol. 1986 Aug 15;35(16):2727-30. doi: 10.1016/0006-2952(86)90181-4.
The levels of hepatic carboxylesterases, including palmitoyl-CoA hydrolase and decanoyl-D,L-carnitine hydrolase, were studied in total homogenates and subcellular fractions prepared from the livers of male rats fed diets containing 0.3% clofibrate. The microsomal carboxylesterase as well as the fatty acyl-thioesterase are differently induced by clofibrate feeding. The specific activities of acetanilide carboxylesterase and decanoyl-D,L-carnitine hydrolase increased more than 3-fold in the microsomal fraction, compared to pellet-fed control animals. The microsomal activities of palmitoyl-CoA hydrolase and propanidid hydrolase were decreased by about 20 to 40% in clofibrate-treated rats. The specific clofibrate hydrolase activity remained unchanged after clofibrate administration, indicating that this microsomal carboxylesterase is not induced by its own substrate. The data suggest a different distribution of the differing carboxylesterase along the endoplasmic reticulum.
对喂食含0.3%氯贝丁酯饲料的雄性大鼠肝脏制备的总匀浆和亚细胞组分中的肝脏羧酸酯酶水平进行了研究，其中包括棕榈酰辅酶A水解酶和癸酰-D,L-肉碱水解酶。氯贝丁酯喂食对微粒体羧酸酯酶以及脂肪酰硫酯酶有不同的诱导作用。与喂食普通饲料的对照动物相比，微粒体组分中乙酰苯胺羧酸酯酶和癸酰-D,L-肉碱水解酶的比活性增加了3倍以上。氯贝丁酯处理的大鼠中，棕榈酰辅酶A水解酶和丙泮尼地水解酶的微粒体活性降低了约20%至40%。给予氯贝丁酯后，氯贝丁酯水解酶的比活性保持不变，表明这种微粒体羧酸酯酶不会被其自身底物诱导。数据表明不同的羧酸酯酶在内质网上有不同的分布。
