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- W2069965802 abstract "A cyclic nucleotide phosphodiesterase (EC 3.1.4.-) has been partially purified from the larvae of silkworm (Bombyx mori). The enzyme catalyzes the hydrolysis of 2′,3′-cyclic nucleotides to 3′-monoesters and 3′,5′-cyclic nucleotides to 5′-monoesters. The 2′,3′-cyclic nucleotide and 3′,5′-cyclic nucleotide phosphodiesterase activities have been purified about 2900- and 2700-fold, respectively. The enzyme preparation is free of phosphomonoesterase, ribonuclease and deoxyribonuclease. Attempts to separate the two activities by a variety of physical and chemical means have been unsuccessful. It is suggested, therefore, that the two activities are associated with the same protein molecule. The enzyme has a molecular weight of 66 000 and does not require the presence of metal ion for its activity. It shows optimum activity at pH 8.2 with 3′,5′-cyclic AMP as substrate and between pH 7.4 and 8.0 with 2′,3′-cyclic AMP as substrate. Both activities are inhibited by caffeine and theophylline." @default.
- W2069965802 created "2016-06-24" @default.
- W2069965802 creator A5066417397 @default.
- W2069965802 date "1974-11-01" @default.
- W2069965802 modified "2023-09-25" @default.
- W2069965802 title "Cyclic nucleotide phosphodiesterase in silkworm: Purification and properties" @default.
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- W2069965802 doi "https://doi.org/10.1016/0005-2744(74)90047-3" @default.
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