Naka A, Yamamoto K, Miwatani T, Honda T
Research Institute for Microbial Diseases, Osaka University, Japan.
FEMS Microbiol Lett. 1992 Nov 1;77(1-3):197-200. doi: 10.1016/0378-1097(92)90155-h.
Two forms (34 kDa and 32 kDa) of hemagglutinin/protease produced by Vibrio cholerae non-O1 were characterized. The hemagglutinin/protease purified by immunoaffinity column chromatography using a monoclonal antibody was essentially a 34-kDa form. By incubation of the purified 34-kDa form at 37 degrees C, it was processed (autodigested) to the 32-kDa form. The N-terminal 20 amino acid sequences of both the 34- and 32-kDa forms were identical, suggesting that proteolytic processing at the C-terminal region of the 34-kDa hemagglutinin/protease resulted in the 32-kDa form. With this shift, protease activity increased, but hemagglutinating activity decreased, suggesting that the C-terminal region of the hemagglutinin/protease is related to hemagglutinating activity.
对霍乱弧菌非O1型产生的两种形式（34 kDa和32 kDa）的血凝素/蛋白酶进行了特性分析。使用单克隆抗体通过免疫亲和柱色谱法纯化的血凝素/蛋白酶基本上是34 kDa的形式。将纯化的34 kDa形式在37℃下孵育，它会被加工（自消化）成32 kDa的形式。34 kDa和32 kDa形式的N端20个氨基酸序列相同，这表明34 kDa血凝素/蛋白酶C端区域的蛋白水解加工产生了32 kDa的形式。随着这种转变，蛋白酶活性增加，但血凝活性降低，这表明血凝素/蛋白酶的C端区域与血凝活性有关。
