Zhukovskiĭ Iu G, Kuznetsova L P, Sochilina E E
Ukr Biokhim Zh (1978). 1995 Jul-Aug;67(4):40-6.
Cetyltrimethyl ammonium and cetylpyridinium, both being cationic detergents, have been studied for their effect on the catalytic activity of horse blood serum cholinesterase (BuHChE) in reactions of hydrolysis of carbonic acid esters. It is shown that the detergents tested are reversible competitive inhibitors of the reaction of butyryl cholinesterase hydrolysis of butyryl choline, a specific cationic substrate, but in this case they activate enzymic hydrolysis of alpha-naphthylacetate, a nonspecific neutral substrate. Values of constants, describing enzyme binding with a detergent, are estimated both by the degree of inhibition of enzymatic hydrolysis of butyryl choline and by the degree of activation of enzymatic hydrolysis of alpha-naphthylacetate and are practically equal. An assumption is made that in both cases the same complex of BuHChE with a molecule of the detergent is formed. The enzyme, as a constituent of such a complex, possesses different substrate specificity as compared with the initial one.
十六烷基三甲基铵和十六烷基吡啶鎓均为阳离子去污剂，它们对马血清胆碱酯酶（丁酰胆碱酯酶，BuHChE）催化碳酸酯水解反应的活性影响已得到研究。结果表明，所测试的去污剂是丁酰胆碱酯酶水解特定阳离子底物丁酰胆碱反应的可逆竞争性抑制剂，但在此情况下，它们会激活非特异性中性底物α-萘乙酸的酶促水解。通过丁酰胆碱酶促水解的抑制程度以及α-萘乙酸酶促水解的激活程度来估算描述酶与去污剂结合的常数，二者实际相等。据此推测，在这两种情况下，BuHChE与去污剂分子形成了相同的复合物。作为这种复合物的组成成分，该酶与初始酶相比具有不同的底物特异性。
