Rathaur S, Misra S, Mohapatra T M, Taneja V
Department of Biochemistry, Banaras Hindu University, Varanasi, India.
Lymphology. 1992 Dec;25(4):159-65.
Setaria cervi, a bovine filarial parasite, contains a significant amount of acetylcholinesterase (AChE) activity with microfilaria having five to ten times more AChE activity than female and male adult worms, respectively. Because AChE shows substrate specificity and hydrolyzes acetylthiocholine but not butrylthiocholine, this parasitic enzyme is likely a true acetylcholinesterase. The latter also resembles an AChE enzyme in the human filarial parasite B. malayi which hydrolyzes acetylthiocholine iodide three times faster than butrylthiocholine iodide. The S. cervi AChE, like its counterpart, also exhibit inhibition with eserine, a specific inhibitor of this enzyme. Subcellular localization of AChE in adult female worms shows enzyme activity both in the mitochondrial and post-mitochondrial fraction. However, enzyme activity in the soluble fraction is twenty-seven times greater than in the mitochondrial fraction.
牛丝状寄生虫鹿丝状线虫含有大量乙酰胆碱酯酶（AChE）活性，其微丝蚴的AChE活性分别比雌性和雄性成虫高五到十倍。由于AChE具有底物特异性，能水解乙酰硫代胆碱而不能水解丁酰硫代胆碱，这种寄生酶可能是一种真正的乙酰胆碱酯酶。后者也类似于人类丝状寄生虫马来布鲁线虫中的一种AChE酶，该酶水解碘化乙酰硫代胆碱的速度比碘化丁酰硫代胆碱快三倍。鹿丝状线虫的AChE与其对应物一样，也会受到该酶的特异性抑制剂毒扁豆碱的抑制。成年雌性线虫中AChE的亚细胞定位显示，线粒体和线粒体后部分均有酶活性。然而，可溶性部分的酶活性比线粒体部分高27倍。
