Thermostable Proteinases from a Luminous Bacterium, Vibrio logei Strain CPM-D3. Purification and Some Properties
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概要
- 論文の詳細を見る
Two proteinases (I and II) from an intestinal luminous bacterium, Vivrio logei strain CPM-D3,were purified. The molecular weights of the proteinases I and II were estimated to be 62000 and 54000,respectively. These enzymes were most active at pH 9.0 and 60℃ (proteinase I) and 50℃ (proteinase II), respectively. These enzyme activities were inhibited by orthophenanthroline, but not by ethylenediamine-tetraacetic acid and phosphoramidon. Metal ions such as Cu^<2+>, Hg^<2+> and Ni<2+> also inhibited these enzyme activities. Both enzyme activities were not affected by heat treatment at 100℃ for 30min.
- 公益社団法人日本薬学会の論文
- 1990-06-25
著者
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倉田 宗司
Department of Physiological Chemistry, Faculty of PharmaceuticalSciences, Josai University
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佐藤 里恵
Laboratory Of Biochemistry Department Of Chemistry Faculty Of Science:josai University
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深沢 茂樹
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science
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武井 繁夫
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science
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嶋 英邦
Pharmacology Research, Fuji Chemical Industries, Ltd.,
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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 Chemistry Faculty Of Science:josai University Sakado
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嶋 英邦
Pharmacology Research Fuji Chemical Institutes Ltd.
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武井 繁夫
Laboratory Of Biochemistry Department Of Chemistry Faculty Of Science:josai University
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