Bózner P, Demes P
Department of Microbiology and Immunology, Comenius University, Bratislava, Czechoslovakia.
Arch Oral Biol. 1991;36(10):765-70. doi: 10.1016/0003-9969(91)90043-t.
Proteinases secreted by an axenic strain of Trichomonas tenax were active against native types I, III, IV and V collagens when evaluated by polyacrylamide gel electrophoresis. Degradation of all four collagen types was temperature dependent. Basement membrane type IV collagen was digested most effectively. An inhibition of all collagenolytic activities by a specific inhibitor of cysteine proteinases, E-64, and activation by a reducing agent, dithiothreitol, indicated the involvement of cysteine proteinases of the oral flagellate in the cleavage of collagen.
通过聚丙烯酰胺凝胶电泳评估时，来自口腔毛滴虫无菌菌株分泌的蛋白酶对天然I型、III型、IV型和V型胶原蛋白具有活性。所有四种胶原蛋白类型的降解都与温度有关。基底膜IV型胶原蛋白的消化最为有效。半胱氨酸蛋白酶的特异性抑制剂E-64对所有胶原olytic活性的抑制以及还原剂二硫苏糖醇的激活表明，这种口腔鞭毛虫的半胱氨酸蛋白酶参与了胶原蛋白的裂解。
