Oligonucleotidase Activity of Phosphodiesterase from the Fruit Body of Flammulina velutipes(Biological Chemistry)
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概要
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A phosphodiesterase (EC 3.1.4.1) was purified to homogeneity from the fruit body of Flammulina velutipes. The enzyme had considerable activity toward oligonucleotides. The Km values were 0.66mM for ApA, 2.47mM for (Ap)_2A, and 3.03mM for (Ap)_3A. The enzyme hydrolyzed oligodeoxyribonucleotides as well as oligoribonucleotides. The oligoribonucleotides bearing a phosphate residue at the 3' end were not hydrolyzed by the enzyme. The enzyme hydrolyzed the oligoribonucleotides exonucleolytically from the 3' to 5' end. Thus the PDase of F. velutipes is considered to function in viva as an oligonucleotidase (EC 3.1.13.3), which efficiently converts oligonucleotides to 5'-mononucleotides in the cell.
- 1990-03-23
著者
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Kurosawa Shin-ichi
Department Of Bioscience And Biotechnology Faculty Of Agriculture Shinshu University
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Sen Kikuo
Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University
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Sen Kikuo
Department Of Bioscience And Biotechnology Shinshu University
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SHIMABUKU T.
Department of Bioscience and Biotechnology, Shinshu University
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ISHIZAWA Hiroshi
Department of Bioscience and Biotechnology, Shinshu University
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Shimabuku T.
Department Of Bioscience And Biotechnology Shinshu University
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Ishizawa Hiroshi
Department Of Bioscience And Biotechnology Shinshu University:(present Office)fushimi Kamaboko Co. L
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Sen Kikuo
Department of Bioscience and Biotechnology Faculty of Agriculture, Shinshu University
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ISHIZAWA Hiroshi
Department of Agricultural Chemistry, Shinshu University
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