Properties of the Proteinase from a Luminous Bacterium, Vibrio splendidus ATCC 33125
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概要
- 論文の詳細を見る
A proteinase was purified from the culture supernatant of a marine luminous bacterium, Vibrio splendidus ATCC 33125. The purified enzyme had a molecular weight of 60000. The enzyme was most active at pH 9.0 and 57℃, and was stable below 45℃. The enzyme activity was inhibited by phosphoramidon, ethylenediaminetetraacetic acid and orthophenanthroline. Metal ions such as Cu^<2+>, Hg^<2+> and Ni^<2+> also inhibited the activity. These results indicate that this enzyme is a metal-chelator-sensitive, alkaline proteinase.
- 公益社団法人日本薬学会の論文
- 1989-05-25
著者
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倉田 宗司
Department of Physiological Chemistry, Faculty of PharmaceuticalSciences, Josai University
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高木 謙
Department Of Biochemistry Faculty Of Science:josai University
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倉田 宗司
Department Of Physiological Chemistry Faculty Of Pharmaceutical Sciences:josai University Sakado
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深沢 茂樹
Department of Biochemistry, Faculty of Science
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深沢 茂樹
Department Of Chemistry Faculty Of Science:josai University Sakado
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