Purification and Properties of a Proteinase from a Marine Luminous Bacterium, Vibrio splendidus Strain FLE-2(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 splendidus biotype I strain FLE-2. A proteinase from this strain, with a specific activity 21-fold higher than that of the culture supernatant, was purified to homogeneity. The purified enzyme had a molecular weight of 50,000. The enzyme was most active at pH 8.0 and 55℃, and stable below 35℃. The enzyme activity was completely inhibited by EDTA, orthophenanthrolin and phosphoramidon. Also metal ions such as Cu^<2+>, Hg^<2+>, Ni^<2+>, Cd^<2+> and Co^<2+> inhibited the activity. These results indicate that this enzyme is a metal-chelater-sensitive, 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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Aoki Satoshi
Department of Cardiovascular center, Chiba-Hokusoh Hospital, Nippon Medical School
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OSUMI MASAKO
Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University
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Aoki Satoshi
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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GAWAZAWA Naoko
Department of Biochemistry, Faculty of Science, Josai University
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Gawazawa Naoko
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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