von Deimling O, de Looze S
Hum Genet. 1983;63(3):241-6. doi: 10.1007/BF00284657.
The selective staining of a single butyrylesterase, following isoelectric focusing of red cell lysates from 14 mammalian species, including man, was achieved using the chromogenic substrate N-acetyl-L-alanine-alpha-naphthyl ester. This procedure optimized the identification of this enzyme, and a close correspondence of its properties was observed in all the species investigated. The inhibition profile, using a range of inhibitors, was identical in all cases. Particularly noteworthy was the activation of the enzyme by p-chloromercuribenzoate at low (2-20 x 10(-6) M) concentrations, but inhibition at higher (greater than 10(-3) M) concentrations. The isoelectric points of all samples fell within a narrow range, pI 4.00-4.43. Descriptions of this activity in different animals, under different designations, could be identified in earlier studies, and the enzyme was uniformly designated "butyrylesterase 1". A tetrameric subunit structure, previously established for the human enzyme, was also demonstrated in the case of mouse butyrylesterase 1. A list of diagnostic characteristics for the enzyme was presented, and it was assumed that the 14 enzymes investigated are orthologous. It was not possible to group butyrylesterase 1 with any other known esterase within the system of enzymes recommended by the IUB, and it was proposed that this enzyme be assigned to a new esterase subclass.
使用显色底物N-乙酰-L-丙氨酸-α-萘酯，对包括人类在内的14种哺乳动物的红细胞裂解物进行等电聚焦后，实现了对单一丁酰酯酶的选择性染色。该方法优化了这种酶的鉴定，并且在所研究的所有物种中都观察到其性质的密切对应。在所有情况下，使用一系列抑制剂得到的抑制谱都是相同的。特别值得注意的是，对氯汞苯甲酸在低浓度（2 - 20×10⁻⁶ M）时激活该酶，但在高浓度（大于10⁻³ M）时抑制该酶。所有样品的等电点都落在一个狭窄的范围内，即pI 4.00 - 4.43。在早期研究中可以识别出不同动物中这种活性在不同名称下的描述，并且该酶被统一命名为“丁酰酯酶1”。先前为人源酶确定的四聚体亚基结构，在小鼠丁酰酯酶1的情况下也得到了证实。列出了该酶的诊断特征清单，并假定所研究的14种酶是直系同源的。在国际生物化学与分子生物学联盟推荐的酶系统中，无法将丁酰酯酶1与任何其他已知酯酶归为一类，因此建议将该酶归入一个新的酯酶亚类。
