Some Properties of Two Proteinases from a Lumonious Bacterium, Vibrio harveyi Strain FLN-108(Biological Chemistry)
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概要
- 論文の詳細を見る
Two proteinase (I and II) from a marine luminous bacterium, FLN-108, were purified to homogeneity. The molecular weights of proteinases I and II were estimated to be 49,000 and 46,000, comprising a dimer of 23,000 molecular weight subunits, respectively. These enzymes were most active at from pH 8.0 to pH 9.0 and 50℃, and stable below 45℃. These enzyme activities were inhibited by EDTA and orthophenanthrolin. Phosphoramidon inhibited the activity of proteinase II, but not that of proteinase I. Metal ions such as Cu^<2+>, Hg^<2+>, and Ni^<2+> strongly inhibited these activities. These results indicate that the proteinases I and II are metal-chelater-sensitive, alkaline proteinases.
- 社団法人日本農芸化学会の論文
- 1988-12-23
著者
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Nakamura Kenji
Department of Surgery, Tokai University School of Medicine
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Nakamura Kenji
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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MIYAHIRA Masaru
Department of Biochemistry, Faculty of Science, Josai University
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KURATA Munetsugu
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Josai University
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Miyahira M
Josai Univ. Sakado Jpn
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Nakamura Kenji
Department Of Anatomy Graduate School Of Medicine Osaka City University
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Miyahira Masaru
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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Kurata Munetsugu
Department Of Physiological Chemistry Faculty Of Pharmaceutical Sciences Josai University
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KURATA Munetsugu
Department of Pharmacy, University Hospital, School of Medicine:Faculty of Pharmaceutical Sciences, The University of Tokushima:Faculty of Pharmaceutical Sciences, Josai University
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