Purification and Properties of a Proteinase from a Marine Luminous Bacterium, Vibrio harveyi Strain FLA-11(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
A proteolytic, marine luminous bacterium was isolated from seawater and identified as Vibrio harveyi strain FLA-11. A proteinase from this strain, with a specificactivity 61-fold higher than that of the culture supernatant, was purified to homogeneity. The purified enzyme had a molecular weight of 84,000, comprising a tetramer of 21,000 molecular weight subunits. The enzyme was most active at pH 8.0 and 55℃, and stable below 40℃. The enzyme activity was completely inhibited by EDTA, orthophenanthrolin and phosphoramidon. Metal ions such as Cu^<2+>, Hg^<2+>, Ni^<2+>, Cd^<2+> and Co^<2+> also inhibited the activity. These results indicate that this enzyme is a metal-chelatersensitive, alkaline proteinase.
- 社団法人日本農芸化学会の論文
- 1988-02-23
著者
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Nakamura Kenji
Department of Surgery, Tokai University School of Medicine
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OSUMI MASAKO
Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University
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Kamii Atsushi
Department Of Biochemistry Faculty Of Science Josai University
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FUKASAWA Shigeki
Department of Biochemistry, Faculty of Science, Josai University
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Nakamura Kenji
Department Of Anatomy Graduate School Of Medicine Osaka City University
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OHYAMA Yoshitaka
Department of Biochemistry, Faculty of Science, Josai University
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Fukasawa Shigeki
Department Of Biochemistry Faculty Of Science Josai University
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Osumi Masako
Department Of Biology Faculty Of Science Osaka City University
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Ohyama Yoshitaka
Department Of Biochemistry Faculty Of Science Josai University
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