Nakasone Noboru, Toma Claudia, Song Tianyan, Iwanaga Masaaki
Division of Bacterial Pathogenesis, Department of Microbiology, Graduate School of Medicine, University of the Ryukyus, 207 Uehara, Okinawa 903-0215, Japan.
FEMS Microbiol Lett. 2004 Aug 1;237(1):127-32. doi: 10.1016/j.femsle.2004.06.025.
A novel protease produced by Aeromonas caviae was purified and characterized. The molecular weight of the protease (AP19) was estimated as 19 kDa on SDS-polyacrylamide gel electrophoresis. The protease activity was not inhibited completely by heating at 100 degrees C for 15 min. The proteolytic activities were inhibited by metalloprotease inhibitor. The N-terminal amino acid sequence of AP19 was VTASVSFSGRCTN. AP19 did not activate Aeromonas proaerolysin, and did not show fluid accumulation in the rabbit intestinal loop test. A high concentration of the protease showed cytotoxic activity against Vero cells.
对豚鼠气单胞菌产生的一种新型蛋白酶进行了纯化和特性鉴定。在SDS-聚丙烯酰胺凝胶电泳上，该蛋白酶（AP19）的分子量估计为19 kDa。蛋白酶活性在100℃加热15分钟后并未被完全抑制。其蛋白水解活性受到金属蛋白酶抑制剂的抑制。AP19的N端氨基酸序列为VTASVSFSGRCTN。AP19不能激活气单胞菌前气溶素，并且在兔肠袢试验中未显示液体蓄积。高浓度的该蛋白酶对Vero细胞表现出细胞毒性活性。
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