Purification and Characterization of an Alkaline Protease from Oerskovia xanthineolytica TK-1
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概要
- 論文の詳細を見る
Alkaline protease from Oerskovia xanthineolytica TK-1 was purified to an electrophoretically homogeneous state by phenyl-Sepharose CL-4B and DEAE-Sephacel. The molecular mass of the enzyme was 20,000 Da by SDS-polyacrylamide gel electrophoresis. The enzyme was most active at pH 9.5-11.0 and 50℃. It was inhibited by inhibitors of serine protease. The enzyme preferentially hydrolyzed the ester of phenylalanine among N-CBZ amino acid p-nitrophenol esters. These results indicate that the protease can be classified as an alkaline serine protease.
- 社団法人日本生物工学会の論文
- 1994-05-25
著者
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Watanabe Yasuo
Department of Cardiology, Nihon University School of Medicine
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Watanabe Yasuo
Department Of Cardiology Nihon University School Of Medicine
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Watanabe Y
Department Of Bioresources Faculty Of Agriculture Ehime University
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TAMAI YOUICHI
Department of Biological Resources, Faculty of Agriculture, Ehime University
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Iwata Junko
Department Of Bioresources Faculty Of Agriculture Ehime University
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Tamai Y
Department Of Bioresources Faculty Of Agriculture Ehime University
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Tamai Youichi
Department Of Agricultural Chemistry College Of Agriculture Ehime University
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Watanabe Y
Department Of Cell Physiology Faculty Of Medicine Kagawa University
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SAEKI KAZUO
Department of Bioresource, Faculty of Agriculture, Ehime University
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Saeki Kazuo
Department Of Bioresources Faculty Of Agriculture Ehime University
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Watanabe Yasuo
Department Of Agricultural Chemistry College Of Agriculture Ehime University
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Watanabe Yasuo
Institute of Space and Astronautical Science
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