Coombs G H
Parasitology. 1982 Feb;84(1):149-55. doi: 10.1017/s003118200005174x.
The amastigote form of the human pathogen Leishmania mexicana contains high proteinase activity, some 20 times greater than that in the promastigote form and macrophages and appreciably higher than the activity in other flagellate protozoa. The main amastigote enzymes are soluble, whereas those of the promastigote are particulate, and have inhibitor sensitivities characteristic of cysteine proteinases. The very high soluble proteinase activity of L. mexicana amastigotes may be a primary factor in the survival and growth of this mammalian stage in its potentially degradative intracellular habitat.
人类病原体墨西哥利什曼原虫的无鞭毛体形式含有高蛋白酶活性，约为前鞭毛体形式和巨噬细胞的20倍，明显高于其他鞭毛虫原生动物的活性。主要的无鞭毛体酶是可溶的，而前鞭毛体的酶是颗粒状的，并且具有半胱氨酸蛋白酶特有的抑制剂敏感性。墨西哥利什曼原虫无鞭毛体极高的可溶性蛋白酶活性可能是该哺乳动物阶段在其潜在的可降解细胞内栖息地中生存和生长的主要因素。
