An Extracellular Protease Produced by Vibrio anguillarum

Abstract

The toxicity of extracellular products (ECP) of Vibrlo anguillarum proved to consist in a protease. The extracellular protease was purified by precipitation with ammonium sulfate and gel filtration, and it showed the following characteristics: 1. The LD50values of the purified protease to goldfish and mouse were 1.7 and 1.6μg pro tein/g weight, respectively. 2. The molecular weight of the purified protease was estimated to be 36,000 by SDS-poly acrylamide gel electrophoresis. 3. Three serotypes of V. anguillarum produced a common protease in antigenicity. 4. The optimum pH and temperature for the activity of the enzyme was 7~8 and 50°C, re spectively. 5. The protease was inhibited by ethylenediaminetetraacetic acid (EDTA). © 1985, The Japanese Society of Fisheries Science. All rights reserved.