Pappas P W
J Parasitol. 1980 Dec;66(6):914-9.
Following electrophoresis of isolated, brush-border membranes of Hymenolepis diminuta on SDS-polyacrylamide gels, three distinct areas of alpha-naphthyl phosphate (NP) hydrolysis were detected; these corresponded to proteins with molecular weights of 106,800, 172,700, and greater than 340,000 Daltons. Hydrolysis of NP was inhibited by adenosine triphosphate, adenosine;5'-monophosphate, p-nitrophenyl-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-diphosphate, molybdate, ethylenediaminetetraacetate (EDTA), and ethyleneglycol-bis-(beta-amino-ethyl)-N,N'-tetraacetate (EGTA), but not by fluoride. Inhibition of NP hydrolysis by EDTA was relieved in the presence of Mg++ or Ca++. Heating the isolated, brush-border membrane in the presence of SDS for 5 min at 95 C destroyed all enzymatic activity. These characteristics indicated that the enzyme(s) responsible for NP hydrolysis (following separation of membrane proteins by SDS-polyacrylamide gel electrophoresis) were the same enzymes responsible for the phosphohydrolase activity associated with intact and solubilized, brush-border membrane preparations of H. diminuta.
在对微小膜壳绦虫分离的刷状缘膜进行十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳后，检测到三个不同的α - 萘基磷酸酯（NP）水解区域；这些区域对应分子量分别为106,800、172,700和大于340,000道尔顿的蛋白质。三磷酸腺苷、腺苷、5'-单磷酸腺苷、对硝基苯磷酸酯、葡萄糖 - 1 - 磷酸酯、葡萄糖 - 6 - 磷酸酯、果糖 - 6 - 磷酸酯、果糖 - 1,6 - 二磷酸酯、钼酸盐、乙二胺四乙酸（EDTA）和乙二醇双（β - 氨基乙基） - N,N'-四乙酸（EGTA）可抑制NP的水解，但氟化物无此作用。在存在镁离子或钙离子的情况下，EDTA对NP水解的抑制作用得以缓解。在95℃下，于SDS存在的情况下将分离的刷状缘膜加热5分钟会破坏所有酶活性。这些特性表明，负责NP水解的酶（通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳分离膜蛋白后）与微小膜壳绦虫完整和可溶解的刷状缘膜制剂中相关的磷酸水解酶活性的酶相同。
