Maksay G, Tegyey Z, Otvös L
Hoppe Seylers Z Physiol Chem. 1978 Aug;359(8):879-86. doi: 10.1515/bchm2.1978.359.2.879.
Hepatic microsomal esterases of the mouse responsible for the bioactivation of inactive (prodrug) esters of the centrally acting oxazepam were studied. The enzymes are situated on the cytoplasmic side of the microsomes. The esterases are partly solubilized and partly inactivated by homogenization in aqueous glycerol and treatment with deoxycholate. There is good correlation between the rates of hydrolysis and steric constants of the acyl moiety. Substrate binding increases to an optimum with the number of carbon atoms in the acyl moiety and is of hydrophobic nature. An attempt has been made to classify the esterases on the basis of the effect of inhibitors and activators.
对负责中枢作用性奥沙西泮无活性（前体药物）酯生物活化的小鼠肝脏微粒体酯酶进行了研究。这些酶位于微粒体的细胞质一侧。通过在甘油水溶液中匀浆并用脱氧胆酸盐处理，酯酶部分溶解且部分失活。水解速率与酰基部分的空间常数之间存在良好的相关性。底物结合随着酰基部分碳原子数增加而增加至最佳状态，并且具有疏水性质。已尝试根据抑制剂和激活剂的作用对酯酶进行分类。
