Tiliabaev Z
Zh Evol Biokhim Fiziol. 1978 Jul-Aug;14(4):405-7.
It was shown that locust cholinesterase splits various thiocholine esters with different rate. Hydrolysis of p-NPA is due to the effect of carboxylesterase. The latter differs from cholinesterase by a low sensitivity to eserine and cation-containing organophosphorus inhibitor methylsulfomethylate-O-ethyl-S-(beta-ethylmercaptoethyl) methylthiophosphonate, as well as by higher sensitivity to triorthocresylphosphate. The results obtained are discussed in relation to possible differences of the active surface of the enzymes studied.
结果表明,蝗虫胆碱酯酶以不同速率分解各种硫代胆碱酯。对硝基苯乙酸(p-NPA)的水解是由于羧酸酯酶的作用。后者与胆碱酯酶不同,对毒扁豆碱和含阳离子的有机磷抑制剂甲基磺甲基-O-乙基-S-(β-乙基巯基乙基)甲基硫代磷酸酯敏感性低,而对磷酸三邻甲苯酯敏感性高。结合所研究酶活性表面可能存在的差异对所得结果进行了讨论。