Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Purification and Properties of Alkaline Phosphodiesterase from the Fruit Body of Flammulina velutipes
Shin-ichi KUROSAWAMoichiro HAYASHIHiroshi ISHIZAWA
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1984 年 48 巻 2 号 p. 299-305

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An alkaline phosphodiesterase has been purified 2200-fold from the fruit body of Flammulina velutipes. The molecular weight is about 53, 000. The optimum pH for hydrolysis of bis-pnitrophenyl phosphate is 8.0. This phosphodiesterase is stable for 30 min below 40°C and in a pH range from 5.5 to 6.5. The Km values for bis-p-nitrophenyl phosphate and p-nitrophenyl deoxythymidine 5'-phosphate are 0.25mM and 0.09mM, respectively. The enzyme does not hydrolyze RNA and DNA, whereas adenosyl uridine 5'-phosphate is hydrolyzed at a considerable rate. The phosphodiesterase also hydrolyzes NAD, UDP-glucose, and ADP-ribose but does not act on ATP and cyclic AMP.
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© Japan Society for Bioscience, Biotechnology, and Agrochemistry
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