Purification and Some Properties of Nuclease Inhibitor from Monascus purpureus
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概要
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An nuclease inhibitor was isolated from cells of Monascus purpureus after 2 days cultivation, and the inhibitor was released into the culture fluid after 6 days when cell autolysis occurred. The inhibitor was positive in ninhydrin and Anthrone tests. The inhibitor was purified by column chromatographies on Sephadex G-25, Biogel P-2 and DEAE-Sephadex A25, and was homogeneous on disc gel electrophoresis. The molecular weight of the inhibitor was estimated to be about 2500 by Sephadex G-75 gel filtration. The inhibitor reduced the activities of Monascus nuclease (nuclease MP) and nuclease PI, when RNA or heat-denatured DNA was used as substrate, but did not affect nucleotidase activity of either enzyme. Snake venom phosphodiesterase was also inhibited to some extent. The action mode of the inhibitor was noncompetitive inhibition. This inhibitor was named NMP inhibitor.
著者
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Kato Fumio
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Saga University
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Murata Akira
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Saga University
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SARUNO Rinjiro
Laboratory of Applied Microbiology, Faculty of Agriculture, Saga University
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SETOYAMA Tamotsu
Laboratory of Applied Microbiology, Faculty of Agriculture, Saga University
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NAKASHIMA Chikako
Laboratory of Applied Microbiology, Faculty of Agriculture, Saga University
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