Pappas P W
Exp Parasitol. 1987 Aug;64(1):38-47. doi: 10.1016/0014-4894(87)90006-3.
Proteins of the isolated brush border membrane of Hymenolepis diminuta were hydrolyzed in vitro by chymotrypsin, papain, pepsin, subtilopeptidase A (= subtilisin Carlsberg), and trypsin. Neither proteolytic nor amidase activity was demonstrable in the isolated membrane using proteinaceous (casein and hemoglobin) or chromogenic (benzoyl-arginine-p-nitroanilide and succinyl-alanyl-alanyl-propyl-phenylalanine p-nitroanilide) substrates, and the membrane preparation did not inhibit the proteolytic and amidase activities of these enzymes. Thus, the isolated tegumental membrane of H. diminuta is not inherently resistant to the action of proteolytic enzymes, and it does not inhibit proteolytic activity. In control incubations containing only buffer, the alkaline phosphatase activity of the brush border membrane decreased in a time dependent manner, but in the presence of chymotrypsin, subtilopeptidase A, and trypsin, the membrane retained greater alkaline phosphatase activity (pepsin and papain could not be tested for this effect on alkaline phosphatase activity). A similar time dependent decrease in activity was also noted for each of the proteolytic enzymes in control assays, but subtilopeptidase A and papain retained greater activity in the presence of the isolated membrane preparation when these assays were compared to controls.
微小膜壳绦虫分离的刷状缘膜蛋白在体外被胰凝乳蛋白酶、木瓜蛋白酶、胃蛋白酶、枯草杆菌肽酶A（= 枯草杆菌蛋白酶卡尔伯格）和胰蛋白酶水解。使用蛋白质类底物（酪蛋白和血红蛋白）或生色底物（苯甲酰精氨酸对硝基苯胺和琥珀酰丙氨酰丙氨酰丙基苯丙氨酸对硝基苯胺）时，在分离的膜中未检测到蛋白水解活性或酰胺酶活性，且膜制剂未抑制这些酶的蛋白水解和酰胺酶活性。因此，微小膜壳绦虫分离的皮层膜本身对蛋白水解酶的作用并无抗性，也不抑制蛋白水解活性。在仅含缓冲液的对照孵育中，刷状缘膜的碱性磷酸酶活性随时间呈下降趋势，但在胰凝乳蛋白酶、枯草杆菌肽酶A和胰蛋白酶存在的情况下，该膜保留了更高的碱性磷酸酶活性（无法检测胃蛋白酶和木瓜蛋白酶对碱性磷酸酶活性的这种影响）。在对照试验中，每种蛋白水解酶的活性也出现了类似的随时间下降的情况，但与对照相比，当这些试验在有分离的膜制剂存在时，枯草杆菌肽酶A和木瓜蛋白酶保留了更高的活性。
