Some Properties of Two Proteinases from a Luminous Bacterium,Vibrio harveyi Strain FLN-108 |
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Authors: | Shigeki Fukasawa Kenji Nakamura Masaru Miyahira Munetsugu Kurata |
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Institution: | 1. Department of Biochemistry, Faculty of Science, Josai University, Sakado, Saitama 350-02, Japan;2. Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Josai University, Sakado, Saitama 350-02, Japan |
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Abstract: | Two proteinases (I and II) from a marine luminous bacterium, FLN-108, were purified to homogeneity. The molecular weights of proteinases I and II were estimated to be 49,000 and 46,000, comprising a dimer of 23,000 molecular weight subunits, respectively. These enzymes were most active at from pH 8.0 to pH 9.0 and 50°C, and stable below 45°C. These enzyme activities were inhibited by EDTA and orthophenanthrolin. Phosphoramidon inhibited the activity of proteinase II, but not that of proteinase I. Metal ions such as Cu2+ , Hg2+ , and Ni2+ strongly inhibited these activities. These results indicate that the proteinases I and II are metal-chelater-sensitive, alkaline proteinases. |
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