Properties of the Proteinase from a Luminous Bacterium, Vibrio harveyi Strain FLN-77

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概要

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• A proteinase from the culture supernatant of marine luminous bacterium, Vibrio harveyi strain FLN-77,was purified. The purified enzyme had a molecular weight of 62000. The enzyme was most active at pH 8.0 and 55℃, and was stable below 45℃. The enzyme activity was completely inhibited by ethylendiaminetetra acetic acid, orthophenanthroline and phosphoramidon. Metal ions such as Cu^<2+>, Hg^<2+> and Ni^<2+> also inhibited the activity. These results indicated that this enzyme is a metal-chelator-sensitive, alkaline proteinase.

• 1989-01-25

著者

• 倉田 宗司

  Department Of Physiological Chemistry Faculty Of Pharmaceutical Sciences:josai University Sakado

• 深澤 茂樹

  Department Of Biochemistry Faculty Of Science Josai University

• 宮原 勝

  Department of Biochemistry, Faculty of Science, Josai University

• 細田 雅代

  Department of Biochemistry, Faculty of Science, Josai University

• 宮原 勝

  Department Of Biochemistry Faculty Of Science Josai University

• 細田 雅代

  Department Of Biochemistry Faculty Of Science Josai University

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