Phosphodiesterase in Microsomes from Bovine Milk |
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Authors: | Setsuro Matsushita Fumio Ibuki Tomohiko Mori Tadao Hata |
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Affiliation: | The Research Institute for Food Science, Kyoto University, Kyoto |
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Abstract: | Phosphodiesterase was solubilized from bovine milk microsomes and partially purified. The purified enzyme showed 20-fold specific activity compared with that of microsomes, and 1,500-fold with that of the original milk.The properties of the enzyme were investigated by using NpT. The pH optimum was at 9.5. The enzyme was inhibited with EDT A and reactivated with the addition of magnesium or calcium ions. This enzyme was strongly inhibited with reducing reagents. Km, value was 7.4 x 10-4 M for NpT at pH 9.5.RNA was hydrolyzed completely to 5′-mononucleotides, and this enzyme may be considered to show the exonucleolytic action for RNA. |
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