Zhukovskiĭ Iu G, Kuznestova L P, Sochilina E E, Fartseĭger A G, Fartseĭger N L, Azliarova M A
Ukr Biokhim Zh (1978). 1994 Sep-Oct;66(5):23-7.
Significant difference in catalytic properties of partially purified cholinesterases from blood serum of pigeon and hen was shown by photometric method using Ellman's reagent. From eight studied thioesters, pigeon cholinesterase hydrolysed with the highest rate butyrylthiocholine but hen cholinesterase--propionylthiocholine. The enzymatic hydrolysis obeyed Michaelis-Menten equation only at low concentration of substrates up to 0.15-0.5 mM. High concentration of substrates activated hen cholinesterase, but inhibited pigeon cholinesterase.
使用埃尔曼试剂的光度法显示，鸽子和母鸡血清中部分纯化的胆碱酯酶的催化特性存在显著差异。在八种研究的硫酯中，鸽子胆碱酯酶对丁酰硫代胆碱的水解速率最高，而母鸡胆碱酯酶对丙酰硫代胆碱的水解速率最高。酶促水解仅在底物浓度低至0.15 - 0.5 mM时符合米氏方程。高浓度底物激活母鸡胆碱酯酶，但抑制鸽子胆碱酯酶。
