- 著者
-
田島 研一
高橋 恒人
絵面 良男
木村 喬久
- 出版者
- 日本水産學會
- 雑誌
- 日本水産学会誌 (ISSN:00215392)
- 巻号頁・発行日
- vol.50, no.1, pp.145-150, 1984
- 被引用文献数
-
1
16
In a previous paper, we examined the toxicity of the extracellular protease of <i>A. salmonicida</i>, Ar-4 (EFDL) on yamabe (<i>Oncorhynchus masou f. ishikawai</i>) and goldfish (<i>Carassius auratus</i>). From these results, we considered the protease secreted by this bacterium was a causative agent of furunculosis.<br> In this paper, we observed enzymatic properties of the purified protease. The results obtained were summarized as follows:<br> 1. The molecular weight of purified protease was estimated to be 71, 000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis.<br> 2. The purified protease showed maximal activity at pH 9.4 and 50°C. It was stable over the pH range 5.0 to 10.0 and was completely inactivated by temperature at 56°C.<br> 3. The protease was presumably classified an alkaline serine protease and it showed chymotryptic properties since it was significantly inhibited by diisopropylfluorophosphate (DFP) and tosyl-phenylalanine-chloromethyl ketone (TPCK) and hydrolyzed <i>N</i>-benzoyl-L-tyrosine ethyl ester (BTEE).